UniProtKB - P0ACJ8 (CRP_ECOLI)
Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>
Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)
- BLAST>sp|P0ACJ8|CRP_ECOLI cAMP-activated global transcriptional regulator CRP OS=Escherichia coli (strain K12) OX=83333 GN=crp PE=1 SV=1 MVLGKPQTDPTLEWFLSHCHIHKYPSKSTLIHQGEKAETLYYIVKGSVAVLIKDEEGKEM ILSYLNQGDFIGELGLFEEGQERSAWVRAKTACEVAEISYKKFRQLIQVNPDILMRLSAQ MARRLQVTSEKVGNLAFLDVTGRIAQTLLNLAKQPDAMTHPDGMQIKITRQEIGQIVGCS RETVGRILKMLEDQNLISAHGKTIVVYGTR
- Align
- Format
- Add to basketAdded to basket
- History
- Other tutorials and videos
- Help video
- Feedback
cAMP-activated global transcriptional regulator CRP
crp
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.8"Transcription of the Escherichia coli adenylate cyclase gene is negatively regulated by cAMP-cAMP receptor protein."
Aiba H.
J. Biol. Chem. 260:3063-3070(1985) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A TRANSCRIPTIONAL REPRESSOR, AUTOREGULATION, DNA-BINDING. - Ref.12"Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP."
Igarashi K., Ishihama A.
Cell 65:1015-1022(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN ACTIVATOR, FUNCTION AS A REPRESSOR, PROBABLE INTERACTION WITH RPOA, SUBUNIT. - Ref.15"Identification of the activating region of catabolite gene activator protein (CAP): isolation and characterization of mutants of CAP specifically defective in transcription activation."
Zhou Y., Zhang X., Ebright R.H.
Proc. Natl. Acad. Sci. U.S.A. 90:6081-6085(1993) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING, MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163. - Ref.16"Characterization of the activating region of Escherichia coli catabolite gene activator protein (CAP). I. Saturation and alanine-scanning mutagenesis."
Niu W., Zhou Y., Dong Q., Ebright Y.W., Ebright R.H.
J. Mol. Biol. 243:595-602(1994) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 1 (AR1), DNA-BINDING, MUTAGENESIS OF ALA-157; THR-159; HIS-160 AND GLY-163. - Ref.17"Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase."
Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.
Cell 87:1123-1134(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 2 (AR2), INTERACTION WITH RPOA, DNA-BINDING, DNA-BENDING, MUTAGENESIS OF HIS-20; HIS-22; LYS-53; GLU-97; LYS-102; THR-159; HIS-160 AND GLY-163. - Ref.19"Transcription activation by the Escherichia coli cyclic AMP receptor protein: determinants within activating region 3."
Rhodius V.A., Busby S.J.
J. Mol. Biol. 299:295-310(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), MUTAGENESIS OF 54-ASP--GLU-56 AND GLU-59. - Ref.20"Interactions between activating region 3 of the Escherichia coli cyclic AMP receptor protein and region 4 of the RNA polymerase sigma(70) subunit: application of suppression genetics."
Rhodius V.A., Busby S.J.
J. Mol. Biol. 299:311-324(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 3 (AR3), PROBABLE INTERACTION WITH SIGMA-70 (RPOD), MUTAGENESIS OF GLU-59. - Ref.22"Identification of the CRP regulon using in vitro and in vivo transcriptional profiling."
Zheng D., Constantinidou C., Hobman J.L., Minchin S.D.
Nucleic Acids Res. 32:5874-5893(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, REGULON, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-102 AND HIS-160. - Ref.23"Studies of the distribution of Escherichia coli cAMP-receptor protein and RNA polymerase along the E. coli chromosome."
Grainger D.C., Hurd D., Harrison M., Holdstock J., Busby S.J.
Proc. Natl. Acad. Sci. U.S.A. 102:17693-17698(2005) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, REGULON. - Ref.24"Study of highly constitutively active mutants suggests how cAMP activates cAMP receptor protein."
Youn H., Kerby R.L., Conrad M., Roberts G.P.
J. Biol. Chem. 281:1119-1127(2006) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF 128-THR-SER-129.
Miscellaneous
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.35"The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer."
Passner J.M., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 94:2843-2847(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH 2 CAMP PER MONOMER AND DNA, SUBUNIT, DNA-BINDING.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.38"Structural basis for cAMP-mediated allosteric control of the catabolite activator protein."
Popovych N., Tzeng S.R., Tonelli M., Ebright R.H., Kalodimos C.G.
Proc. Natl. Acad. Sci. U.S.A. 106:6927-6932(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 2-210 OF APO-CRP, ENZYME REGULATION, SUBUNIT. - Ref.39"Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding."
Sharma H., Yu S., Kong J., Wang J., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 106:16604-16609(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APO-CRP, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ASP-139.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 97 | Activating region 2 (AR2); probably contacts the N-terminus of RpoA | 1 | |
| <p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 102 | Activating region 2 (AR2); probably contacts the N-terminus of RpoA | 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 129 | cAMP6 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 57 – 63 | cAMP 16 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 7 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 72 – 74 | cAMP 16 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 83 – 84 | cAMP 16 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 128 – 129 | cAMP 16 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 136 – 137 | cAMP 26 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi | 171 – 181 | cAMP 26 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 11 | |
| <p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi | 180 – 186 | H-T-H motifPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi | 7 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cAMP binding Source: UniProtKB-KW
- DNA binding transcription factor activity Source: InterPro
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- sequence-specific DNA binding Source: CollecTF <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- carbon catabolite repression of transcription Source: EcoCyc <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of transcription, DNA-templated Source: EcoliWiki <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription, DNA-templated Source: EcoliWiki <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription, DNA-templated Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Activator, DNA-binding, Repressor |
| Biological process | Transcription, Transcription regulation |
| Ligand | cAMP, cAMP-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:PD00257 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: cAMP-activated global transcriptional regulator CRPAlternative name(s): Catabolite activator protein Short name: CAP Catabolite gene activator cAMP receptor protein Short name: CRP cAMP regulatory protein |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:crp Synonyms:cap, csm Ordered Locus Names:b3357, JW5702 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Escherichia coli (strain K12) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 83333 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › Escherichia coli |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Escherichia coli strain K12 genome database More...EcoGenei | EG10164 crp |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti
- cytosol Source: EcoCyc <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein-DNA complex Source: CollecTF <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.6"Deletion of the Escherichia coli crp gene."
Sabourin D., Beckwith J.
J. Bacteriol. 122:338-340(1975) [PubMed] [Europe PMC] [Abstract]Cited for: DISRUPTION PHENOTYPE. - Ref.22"Identification of the CRP regulon using in vitro and in vivo transcriptional profiling."
Zheng D., Constantinidou C., Hobman J.L., Minchin S.D.
Nucleic Acids Res. 32:5874-5893(2004) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, REGULON, DISRUPTION PHENOTYPE, MUTAGENESIS OF LYS-102 AND HIS-160. - Ref.25"Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia coli."
Iwamoto A., Lemire S., Yonesaki T.
Mol. Microbiol. 70:1570-1578(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, DISRUPTION PHENOTYPE.
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 20 | H → A, L or Y: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 22 | H → A or L: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 53 | K → N: Increased activation at class II promoters, increased interaction with RNAP. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 54 – 56 | DEE → AAA: 80% reduction in activation of class II promoters; 95% loss when associated with A-59. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 3 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 59 | E → A: 45% reduction in activation of class II promoters; 95% loss when associated with AAA-54-56. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 59 | E → G or K: Reduction in activation of class II promoters. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 63 | S → A: Enhanced cAMP-binding, enhanced transcription. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 83 | R → L: Loss of cAMP-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 84 | S → A or K: No modification of cAMP-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 97 | E → A: Increased transcription activation at class II promoters, binds DNA. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 102 | K → E: Disrupts AR2. No activation of class II promoters, decreased interaction with RNAP, binds DNA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 128 – 129 | TS → LI: Constitutively active at class I and II promoters in the absence of cAMP, binds DNA almost as well in the absence as in the presence of cAMP. Binds cAMP normally. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 128 | T → A: No modification of cAMP-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 129 | S → A: Reduced DNA-binding; no modification of cAMP-binding. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 139 | D → L: Some stabilization of an inactive (apo-) form. Decreased affinity for DNA, normal subunit association. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 157 | A → D or P: Decreased transcription activation (6-29%), binds DNA. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 159 | T → A, I, N, S or V: Decreased transcription activation (15-87%) at class I and II promoters, binds DNA. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 160 | H → A, K, L, N, P, Q, R or Y: Disrupts AR1. Decreased transcription activation (3-45%) at class I and II promoters, binds DNA. 4 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 163 | G → A, C, D, R, S or V: Decreased transcription activation (2-62%) at class I and II promoters, binds DNA. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 181 | R → K: Suppresses DNA-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 181 | R → L: Suppresses DNA-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 186 | R → K: No modification of DNA-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 186 | R → L: Marginally reduced DNA-binding. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB02527 Cyclic Adenosine Monophosphate |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methioninei | Removed1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| |||
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000100144 | 2 – 210 | cAMP-activated global transcriptional regulator CRPAdd BLAST | 209 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 101 | N6-acetyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
AcetylationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0ACJ8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0ACJ8 |
PRoteomics IDEntifications database More...PRIDEi | P0ACJ8 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P0ACJ8 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"Autoregulation of the Escherichia coli crp gene: CRP is a transcriptional repressor for its own gene."
Aiba H.
Cell 32:141-149(1983) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, NEGATIVE AUTOREGULATION, DNA-BINDING. - Ref.13"A new aspect of transcriptional control of the Escherichia coli crp gene: positive autoregulation."
Hanamura A., Aiba H.
Mol. Microbiol. 6:2489-2497(1992) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, POSITIVE AUTOREGULATION. - Ref.25"Post-transcriptional control of Crp-cAMP by RNase LS in Escherichia coli."
Iwamoto A., Lemire S., Yonesaki T.
Mol. Microbiol. 70:1570-1578(2008) [PubMed] [Europe PMC] [Abstract]Cited for: INDUCTION, DISRUPTION PHENOTYPE.
Gene expression databases
CollecTF database of bacterial transcription factor binding sites More...CollecTFi | EXPREG_00000850 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"Binding of the cyclic AMP receptor protein of Escherichia coli to RNA polymerase."
Pinkney M., Hoggett J.G.
Biochem. J. 250:897-902(1988) [PubMed] [Europe PMC] [Abstract]Cited for: CAMP-BINDING, INTERACTION WITH RNA POLYMERASE, SUBUNIT. - Ref.12"Bipartite functional map of the E. coli RNA polymerase alpha subunit: involvement of the C-terminal region in transcription activation by cAMP-CRP."
Igarashi K., Ishihama A.
Cell 65:1015-1022(1991) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS AN ACTIVATOR, FUNCTION AS A REPRESSOR, PROBABLE INTERACTION WITH RPOA, SUBUNIT. - Ref.17"Transcription activation at class II CAP-dependent promoters: two interactions between CAP and RNA polymerase."
Niu W., Kim Y., Tau G., Heyduk T., Ebright R.H.
Cell 87:1123-1134(1996) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CHARACTERIZATION OF ACTIVATING REGION 2 (AR2), INTERACTION WITH RPOA, DNA-BINDING, DNA-BENDING, MUTAGENESIS OF HIS-20; HIS-22; LYS-53; GLU-97; LYS-102; THR-159; HIS-160 AND GLY-163. - Ref.31"Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP."
McKay D.B., Weber I.T., Steitz T.A.
J. Biol. Chem. 257:9518-9524(1982) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN. - Ref.32"Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5-A resolution."
Weber I.T., Steitz T.A.
J. Mol. Biol. 198:311-326(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN. - Ref.33"Crystal structure of a CAP-DNA complex: the DNA is bent by 90 degrees."
Schultz S., Shields G., Steitz T.A.
Science 253:1001-1007(1991) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-206 IN COMPLEX WITH CAMP AND DNA, SUBUNIT, DNA-BINDING, DNA-BENDING. - Ref.34"Structure of the CAP-DNA complex at 2.5 angstroms resolution: a complete picture of the protein-DNA interface."
Parkinson G., Wilson C., Gunasekera A., Ebright Y.W., Ebright R.H., Berman H.M.
J. Mol. Biol. 260:395-408(1996) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP AND DNA, SUBUNIT, DNA-BINDING, DNA-BENDING. - Ref.35"The structure of a CAP-DNA complex having two cAMP molecules bound to each monomer."
Passner J.M., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 94:2843-2847(1997) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH 2 CAMP PER MONOMER AND DNA, SUBUNIT, DNA-BINDING. - Ref.36"Modeling the cAMP-induced allosteric transition using the crystal structure of CAP-cAMP at 2.1 A resolution."
Passner J.M., Schultz S.C., Steitz T.A.
J. Mol. Biol. 304:847-859(2000) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT. - Ref.37"Structural basis of transcription activation: the CAP-alpha CTD-DNA complex."
Benoff B., Yang H., Lawson C.L., Parkinson G., Liu J., Blatter E., Ebright Y.W., Berman H.M., Ebright R.H.
Science 297:1562-1566(2002) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF 2-210 IN COMPLEX WITH CAMP; DNA AND RNAP, INTERACTION WITH RPOA, DNA-BINDING, SUBUNIT. - Ref.38"Structural basis for cAMP-mediated allosteric control of the catabolite activator protein."
Popovych N., Tzeng S.R., Tonelli M., Ebright R.H., Kalodimos C.G.
Proc. Natl. Acad. Sci. U.S.A. 106:6927-6932(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY NMR OF 2-210 OF APO-CRP, ENZYME REGULATION, SUBUNIT. - Ref.39"Structure of apo-CAP reveals that large conformational changes are necessary for DNA binding."
Sharma H., Yu S., Kong J., Wang J., Steitz T.A.
Proc. Natl. Acad. Sci. U.S.A. 106:16604-16609(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF APO-CRP, ENZYME REGULATION, SUBUNIT, MUTAGENESIS OF ASP-139. - Ref.40"Three-dimensional EM structure of an intact activator-dependent transcription initiation complex."
Hudson B.P., Quispe J., Lara-Gonzalez S., Kim Y., Berman H.M., Arnold E., Ebright R.H., Lawson C.L.
Proc. Natl. Acad. Sci. U.S.A. 106:19830-19835(2009) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (19.80 ANGSTROMS) OF 2-210 IN COMPLEX WITH RPOA; RPOB; RPOC; RPOD; RPOZ AND DNA, INTERACTION WITH ROPA, DNA-BINDING, SUBUNIT. - Ref.41"Crystal structure of activated CRP protein from E.coli."
Kumarevel T.S., Tanaka T., Shinkai A., Yokoyama S.
Submitted (FEB-2009) to the PDB data bankCited for: X-RAY CRYSTALLOGRAPHY (2.21 ANGSTROMS) OF 2-210 IN COMPLEX WITH 2 CAMP PER MONOMER, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| itself | 5 | EBI-547513,EBI-547513 | ||
| nusG | P0AFG0 | 2 | EBI-547513,EBI-369628 | |
| priC | P23862 | 2 | EBI-547513,EBI-1117383 | |
| rplL | P0A7K2 | 2 | EBI-547513,EBI-543702 | |
| yacL | P0A8E5 | 4 | EBI-547513,EBI-554965 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- identical protein binding Source: IntAct <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4262928, 15 interactors |
Database of interacting proteins More...DIPi | DIP-29232N |
Protein interaction database and analysis system More...IntActi | P0ACJ8, 42 interactors |
Molecular INTeraction database More...MINTi | P0ACJ8 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3533 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 4 – 6 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 10 – 16 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 19 – 24 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 25 – 27 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 29 – 31 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 33 – 36 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 39 – 45 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 47 – 53 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 55 – 57 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 59 – 66 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 70 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 74 – 77 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 78 – 80 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 85 – 91 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 93 – 99 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 100 – 109 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 112 – 137 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 26 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 140 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 154 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 158 – 160 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 163 – 167 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 170 – 177 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 181 – 193 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 196 – 200 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 203 – 207 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1CGP | X-ray | 3.00 | A/B | 2-206 | [»] | |
| 1G6N | X-ray | 2.10 | A/B | 1-210 | [»] | |
| 1HW5 | X-ray | 1.82 | A/B | 1-210 | [»] | |
| 1I5Z | X-ray | 1.90 | A/B | 2-210 | [»] | |
| 1I6X | X-ray | 2.20 | A/B | 2-210 | [»] | |
| 1J59 | X-ray | 2.50 | A/B | 2-210 | [»] | |
| 1LB2 | X-ray | 3.10 | A | 2-210 | [»] | |
| 1O3Q | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3R | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3S | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3T | X-ray | 2.80 | A/B | 9-208 | [»] | |
| 1RUN | X-ray | 2.70 | A/B | 2-210 | [»] | |
| 1RUO | X-ray | 2.70 | A/B | 2-210 | [»] | |
| 1ZRC | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRD | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRE | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRF | X-ray | 2.10 | A/B | 2-210 | [»] | |
| 2CGP | X-ray | 2.20 | A | 1-210 | [»] | |
| 2GAP | model | - | A/B | 2-209 | [»] | |
| 2GZW | X-ray | 2.21 | A/B/C/D | 2-210 | [»] | |
| 2WC2 | NMR | - | A/B | 2-210 | [»] | |
| 3FWE | X-ray | 2.30 | A/B | 1-210 | [»] | |
| 3HIF | X-ray | 3.59 | A/B/C/D/E/F | 1-210 | [»] | |
| 3IYD | electron microscopy | - | G/H | 2-210 | [»] | |
| 3KCC | X-ray | 1.66 | A/B | 1-210 | [»] | |
| 3N4M | X-ray | 2.99 | A | 2-210 | [»] | |
| 3QOP | X-ray | 1.96 | A/B | 1-210 | [»] | |
| 3RDI | X-ray | 2.95 | A/B | 1-210 | [»] | |
| 3ROU | X-ray | 2.10 | A/B | 1-210 | [»] | |
| 3RPQ | X-ray | 2.61 | A/B | 1-210 | [»] | |
| 3RYP | X-ray | 1.60 | A/B | 1-210 | [»] | |
| 3RYR | X-ray | 2.70 | A/B | 1-210 | [»] | |
| 4BH9 | NMR | - | A | 2-210 | [»] | |
| 4BHP | NMR | - | A | 2-210 | [»] | |
| 4FT8 | X-ray | 1.97 | A/B | 2-210 | [»] | |
| 4HZF | X-ray | 1.48 | A/B | 1-210 | [»] | |
| 4I01 | X-ray | 2.30 | A/B | 1-210 | [»] | |
| 4I02 | X-ray | 1.75 | A/B/C/D/E/F | 1-210 | [»] | |
| 4I09 | X-ray | 2.05 | A/B | 1-210 | [»] | |
| 4I0A | X-ray | 2.20 | A/B | 1-210 | [»] | |
| 4I0B | X-ray | 1.50 | A/B | 1-210 | [»] | |
| 4R8H | X-ray | 1.46 | A/B | 1-210 | [»] | |
| 5CIZ | X-ray | 5.01 | A | 2-210 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0ACJ8 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0ACJ8 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0ACJ8 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 138 – 210 | HTH crp-typePROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 73 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 20 – 22 | Activating region 2 (AR2); probably contacts the N-terminus of RpoA | 3 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 53 – 59 | Activating region 3 (AR3); probably contacts sigma-70 (RpoD) | 7 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 154 – 163 | Activating region 1 (AR1); probably contacts the C-terminus of RpoA | 10 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.31"Structure of catabolite gene activator protein at 2.9-A resolution. Incorporation of amino acid sequence and interactions with cyclic AMP."
McKay D.B., Weber I.T., Steitz T.A.
J. Biol. Chem. 257:9518-9524(1982) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN. - Ref.32"Structure of a complex of catabolite gene activator protein and cyclic AMP refined at 2.5-A resolution."
Weber I.T., Steitz T.A.
J. Mol. Biol. 198:311-326(1987) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH CAMP, SUBUNIT, DOMAIN.
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0664 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000250565 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0ACJ8 |
KEGG Orthology (KO) More...KOi | K10914 |
Identification of Orthologs from Complete Genome Data More...OMAi | TECEVAE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0ACJ8 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00038 CAP_ED, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.10, 1 hit 2.60.120.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR018490 cNMP-bd-like IPR018488 cNMP-bd_CS IPR000595 cNMP-bd_dom IPR012318 HTH_CRP IPR014710 RmlC-like_jellyroll IPR018335 Tscrpt_reg_HTH_Crp-type_CS IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00027 cNMP_binding, 1 hit PF00325 Crp, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00034 HTHCRP |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00100 cNMP, 1 hit SM00419 HTH_CRP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46785 SSF46785, 1 hit SSF51206 SSF51206, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00888 CNMP_BINDING_1, 1 hit PS00889 CNMP_BINDING_2, 1 hit PS50042 CNMP_BINDING_3, 1 hit PS00042 HTH_CRP_1, 1 hit PS51063 HTH_CRP_2, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
10 20 30 40 50
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV
60 70 80 90 100
LIKDEEGKEM ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY
110 120 130 140 150
KKFRQLIQVN PDILMRLSAQ MARRLQVTSE KVGNLAFLDV TGRIAQTLLN
160 170 180 190 200
LAKQPDAMTH PDGMQIKITR QEIGQIVGCS RETVGRILKM LEDQNLISAH
210
GKTIVVYGTR
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 29 | T → K in BAE77933 (PubMed:16738553).Curated | 1 |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J01598 Genomic DNA Translation: AAA23601.1 U18997 Genomic DNA Translation: AAA58154.1 U00096 Genomic DNA Translation: AAC76382.1 AP009048 Genomic DNA Translation: BAE77933.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A93416 QRECC |
NCBI Reference Sequences More...RefSeqi | NP_417816.1, NC_000913.3 WP_000242755.1, NZ_CP014272.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76382; AAC76382; b3357 BAE77933; BAE77933; BAE77933 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 33939152 947867 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW5702 eco:b3357 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3373 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0ACJ8 | cAMP-activated global transcriptional regulator CRP | 210 | |||
| cAMP-activated global transcriptional regulator CRP | 210 | ||||
| cAMP-activated global transcriptional regulator CRP | 210 | ||||
| DNA-binding transcriptional dual regulator | 210 | ||||
| Cyclic AMP receptor protein | 210 | ||||
| +209 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0ACJ8 | cAMP-activated global transcriptional regulator CRP | 210 | |||
| cAMP-activated global transcriptional regulator CRP | 210 | ||||
| cAMP-activated global transcriptional regulator CRP | 210 | ||||
| DNA-binding transcriptional dual regulator | 210 | ||||
| Cyclic AMP receptor protein | 210 | ||||
| +956 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0ACJ8 | cAMP-activated global transcriptional regulator CRP | 224 | |||
| Transcriptional regulator, Crp/Fnr family | 224 | ||||
| Cyclic AMP receptor protein | 224 | ||||
| cAMP-regulatory protein | 224 | ||||
| cAMP-regulatory protein | 224 | ||||
| +1517 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | J01598 Genomic DNA Translation: AAA23601.1 U18997 Genomic DNA Translation: AAA58154.1 U00096 Genomic DNA Translation: AAC76382.1 AP009048 Genomic DNA Translation: BAE77933.1 |
Protein sequence database of the Protein Information Resource More...PIRi | A93416 QRECC |
NCBI Reference Sequences More...RefSeqi | NP_417816.1, NC_000913.3 WP_000242755.1, NZ_CP014272.1 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1CGP | X-ray | 3.00 | A/B | 2-206 | [»] | |
| 1G6N | X-ray | 2.10 | A/B | 1-210 | [»] | |
| 1HW5 | X-ray | 1.82 | A/B | 1-210 | [»] | |
| 1I5Z | X-ray | 1.90 | A/B | 2-210 | [»] | |
| 1I6X | X-ray | 2.20 | A/B | 2-210 | [»] | |
| 1J59 | X-ray | 2.50 | A/B | 2-210 | [»] | |
| 1LB2 | X-ray | 3.10 | A | 2-210 | [»] | |
| 1O3Q | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3R | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3S | X-ray | 3.00 | A | 9-208 | [»] | |
| 1O3T | X-ray | 2.80 | A/B | 9-208 | [»] | |
| 1RUN | X-ray | 2.70 | A/B | 2-210 | [»] | |
| 1RUO | X-ray | 2.70 | A/B | 2-210 | [»] | |
| 1ZRC | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRD | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRE | X-ray | 2.80 | A/B | 2-210 | [»] | |
| 1ZRF | X-ray | 2.10 | A/B | 2-210 | [»] | |
| 2CGP | X-ray | 2.20 | A | 1-210 | [»] | |
| 2GAP | model | - | A/B | 2-209 | [»] | |
| 2GZW | X-ray | 2.21 | A/B/C/D | 2-210 | [»] | |
| 2WC2 | NMR | - | A/B | 2-210 | [»] | |
| 3FWE | X-ray | 2.30 | A/B | 1-210 | [»] | |
| 3HIF | X-ray | 3.59 | A/B/C/D/E/F | 1-210 | [»] | |
| 3IYD | electron microscopy | - | G/H | 2-210 | [»] | |
| 3KCC | X-ray | 1.66 | A/B | 1-210 | [»] | |
| 3N4M | X-ray | 2.99 | A | 2-210 | [»] | |
| 3QOP | X-ray | 1.96 | A/B | 1-210 | [»] | |
| 3RDI | X-ray | 2.95 | A/B | 1-210 | [»] | |
| 3ROU | X-ray | 2.10 | A/B | 1-210 | [»] | |
| 3RPQ | X-ray | 2.61 | A/B | 1-210 | [»] | |
| 3RYP | X-ray | 1.60 | A/B | 1-210 | [»] | |
| 3RYR | X-ray | 2.70 | A/B | 1-210 | [»] | |
| 4BH9 | NMR | - | A | 2-210 | [»] | |
| 4BHP | NMR | - | A | 2-210 | [»] | |
| 4FT8 | X-ray | 1.97 | A/B | 2-210 | [»] | |
| 4HZF | X-ray | 1.48 | A/B | 1-210 | [»] | |
| 4I01 | X-ray | 2.30 | A/B | 1-210 | [»] | |
| 4I02 | X-ray | 1.75 | A/B/C/D/E/F | 1-210 | [»] | |
| 4I09 | X-ray | 2.05 | A/B | 1-210 | [»] | |
| 4I0A | X-ray | 2.20 | A/B | 1-210 | [»] | |
| 4I0B | X-ray | 1.50 | A/B | 1-210 | [»] | |
| 4R8H | X-ray | 1.46 | A/B | 1-210 | [»] | |
| 5CIZ | X-ray | 5.01 | A | 2-210 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0ACJ8 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0ACJ8 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 4262928, 15 interactors |
Database of interacting proteins More...DIPi | DIP-29232N |
Protein interaction database and analysis system More...IntActi | P0ACJ8, 42 interactors |
Molecular INTeraction database More...MINTi | P0ACJ8 |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3533 |
Chemistry databases
Drug and drug target database More...DrugBanki | DB02527 Cyclic Adenosine Monophosphate |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P0ACJ8 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P0ACJ8 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0ACJ8 |
PRoteomics IDEntifications database More...PRIDEi | P0ACJ8 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76382; AAC76382; b3357 BAE77933; BAE77933; BAE77933 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 33939152 947867 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW5702 eco:b3357 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3373 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB0162 |
Escherichia coli strain K12 genome database More...EcoGenei | EG10164 crp |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0664 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000250565 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0ACJ8 |
KEGG Orthology (KO) More...KOi | K10914 |
Identification of Orthologs from Complete Genome Data More...OMAi | TECEVAE |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0ACJ8 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:PD00257 |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0ACJ8 |
Protein Ontology More...PROi | PR:P0ACJ8 |
Gene expression databases
CollecTF database of bacterial transcription factor binding sites More...CollecTFi | EXPREG_00000850 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00038 CAP_ED, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.10, 1 hit 2.60.120.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR018490 cNMP-bd-like IPR018488 cNMP-bd_CS IPR000595 cNMP-bd_dom IPR012318 HTH_CRP IPR014710 RmlC-like_jellyroll IPR018335 Tscrpt_reg_HTH_Crp-type_CS IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00027 cNMP_binding, 1 hit PF00325 Crp, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00034 HTHCRP |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00100 cNMP, 1 hit SM00419 HTH_CRP, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46785 SSF46785, 1 hit SSF51206 SSF51206, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00888 CNMP_BINDING_1, 1 hit PS00889 CNMP_BINDING_2, 1 hit PS50042 CNMP_BINDING_3, 1 hit PS00042 HTH_CRP_1, 1 hit PS51063 HTH_CRP_2, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | CRP_ECOLI | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P0ACJ8Primary (citable) accession number: P0ACJ8 Secondary accession number(s): P03020, Q2M723 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
| Last sequence update: | July 21, 1986 | |
| Last modified: | March 28, 2018 | |
| This is version 116 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Escherichia coli
Escherichia coli (strain K12): entries and cross-references to EcoGene - PDB cross-references
Index of Protein Data Bank (PDB) cross-references
