UniProtKB - P0AEE3 (DEGS_ECOLI)
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- BLAST>sp|P0AEE3|DEGS_ECOLI Serine endoprotease DegS OS=Escherichia coli (strain K12) OX=83333 GN=degS PE=1 SV=1 MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVN VYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVG SDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIG LNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQL ATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQV NDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN
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Serine endoprotease DegS
degS
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.7"The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor."
Ades S.E., Connolly L.E., Alba B.M., Gross C.A.
Genes Dev. 13:2449-2461(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-201. - Ref.8"degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity."
Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.
Mol. Microbiol. 40:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE. - Ref.9"YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA."
Kanehara K., Ito K., Akiyama Y.
Genes Dev. 16:2147-2155(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE. - Ref.10"DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response."
Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.
Genes Dev. 16:2156-2168(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE. - Ref.11"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN. - Ref.12"Inhibition of regulated proteolysis by RseB."
Cezairliyan B.O., Sauer R.T.
Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, DOMAIN. - Ref.13"A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli."
Inaba K., Suzuki M., Maegawa K., Akiyama S., Ito K., Akiyama Y.
J. Biol. Chem. 283:35042-35052(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, FUNCTION AS A SENSOR. - Ref.14"Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage."
Li X., Wang B., Feng L., Kang H., Qi Y., Wang J., Shi Y.
Proc. Natl. Acad. Sci. U.S.A. 106:14837-14842(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, FUNCTION AS A SENSOR. - Ref.15"Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli."
Meltzer M., Hasenbein S., Mamant N., Merdanovic M., Poepsel S., Hauske P., Kaiser M., Huber R., Krojer T., Clausen T., Ehrmann M.
Res. Microbiol. 160:660-666(2009) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A REGULATORY PROTEASE. - Ref.20"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."
Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J., Kirk R., Hasenbein S., Ehrmann M., Clausen T.
Genes Dev. 21:2659-2670(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ENZYME REGULATION, BINDING OF PEPTIDE, SUBUNIT, MUTAGENESIS OF ASP-122 AND TYR-162.
Miscellaneous
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<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.11"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN. - Ref.12"Inhibition of regulated proteolysis by RseB."
Cezairliyan B.O., Sauer R.T.
Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, DOMAIN. - Ref.20"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."
Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J., Kirk R., Hasenbein S., Ehrmann M., Clausen T.
Genes Dev. 21:2659-2670(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ENZYME REGULATION, BINDING OF PEPTIDE, SUBUNIT, MUTAGENESIS OF ASP-122 AND TYR-162. - Ref.21"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.22"Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution."
Sohn J., Grant R.A., Sauer R.T.
J. Biol. Chem. 285:34039-34047(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-256 OF MUTANT ALA-162; ALA-178; ALA-191: GLN-198, MUTAGENESIS OF TYR-162; ARG-178; GLN-191 AND HIS-198, ENZYME REGULATION, SUBUNIT, ACTIVE SITE.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=33 µM for RseA-YQF2 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
- Ref.19"Allosteric activation of DegS, a stress sensor PDZ protease."
Sohn J., Grant R.A., Sauer R.T.
Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.21"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
- Vmax=0.6 µmol/sec/mg enzyme2 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
- Ref.19"Allosteric activation of DegS, a stress sensor PDZ protease."
Sohn J., Grant R.A., Sauer R.T.
Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.21"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 96 | Charge relay system3 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 ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 126 | Charge relay system3 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 ‘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 | 184 | Substrate | 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 201 | Charge relay system3 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 ‘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 | 351 | Substrate | 1 |
<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
- peptidase activity Source: EcoliWiki <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
- serine-type endopeptidase activity 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
- serine-type peptidase activity Source: EcoliWiki <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
<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
- cellular response to misfolded protein 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
- proteolysis 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
<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 | Hydrolase, Protease, Serine protease |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11652-MONOMER MetaCyc:EG11652-MONOMER |
Protein family/group databases
MEROPS protease database More...MEROPSi | S01.275 |
<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: Serine endoprotease DegS (EC:3.4.21.107)Alternative name(s): Site-1 protease DegS Short name: S1P protease DegS Site-1-type intramembrane protease |
| <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:degS Synonyms:hhoB, htrH Ordered Locus Names:b3235, JW3204 |
| <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 | EG11652 degS |
<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
- Cell inner membrane 1 Publication
<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.8"degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity."
Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.
Mol. Microbiol. 40:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
<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.8"degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity."
Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.
Mol. Microbiol. 40:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
Note: It is unclear how this protein is anchored to the inner membrane, programs predict a signal sequence, but replacing the N-terminal 26 residues with a known signal sequence gives a protein unable to fully complement a disruption mutant.1 Publication - Ref.8"degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity."
Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.
Mol. Microbiol. 40:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE.
<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
Topology
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 4 | Cytoplasmic1 Publication <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
| 4 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 5 – 27 | HelicalSequence analysisAdd BLAST | 23 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 28 – 355 | Periplasmic1 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
| 328 |
<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
- integral component of external side of plasma membrane Source: EcoliWiki <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
- outer membrane-bounded periplasmic space 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>Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Membrane<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.2"Characterization of degQ and degS, Escherichia coli genes encoding homologs of the DegP protease."
Waller P.R., Sauer R.T.
J. Bacteriol. 178:1146-1153(1996) [PubMed] [Europe PMC] [Abstract]Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, NOMENCLATURE. - Ref.7"The Escherichia coli sigma(E)-dependent extracytoplasmic stress response is controlled by the regulated proteolysis of an anti-sigma factor."
Ades S.E., Connolly L.E., Alba B.M., Gross C.A.
Genes Dev. 13:2449-2461(1999) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, DISRUPTION PHENOTYPE, MUTAGENESIS OF SER-201. - Ref.8"degS (hhoB) is an essential Escherichia coli gene whose indispensable function is to provide sigma (E) activity."
Alba B.M., Zhong H.J., Pelayo J.C., Gross C.A.
Mol. Microbiol. 40:1323-1333(2001) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, DISRUPTION PHENOTYPE. - Ref.9"YaeL (EcfE) activates the sigma(E) pathway of stress response through a site-2 cleavage of anti-sigma(E), RseA."
Kanehara K., Ito K., Akiyama Y.
Genes Dev. 16:2147-2155(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, DISRUPTION PHENOTYPE. - Ref.10"DegS and YaeL participate sequentially in the cleavage of RseA to activate the sigma(E)-dependent extracytoplasmic stress response."
Alba B.M., Leeds J.A., Onufryk C., Lu C.Z., Gross C.A.
Genes Dev. 16:2156-2168(2002) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, 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 | 122 | D → A: Causes substantial reduction of peptidase activity. Binds activator peptides. 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 | 162 | Y → A: Loss of peptidase activity. Binds activator peptides. 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 | 162 | Y → F: Loss of 60% of peptidase activity. 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 | 178 | R → A: Causes substantial reduction of peptidase activity. 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 | 183 | P → A: Loss of peptidase activity. Also affects an interface contact between the PDZ and protease domains. 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 | 191 | Q → A: Loss of peptidase activity. 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 | 198 | H → A: Behaves like wild-type. 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 | 198 | H → P: Partially bypasses the requirement for peptide activation, acts synergistically with mutations that disrupt contacts between the protease and PDZ domains and with an rseB disruption. 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 | 201 | S → A: Does not restore RseA degradation in a degS disruption. Loss of RseA degradation. 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 | 227 | E → A: Loss of peptidase activity. 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 | 243 | K → D: Increases the basal rate of RseA cleavage 3-fold, acts synergistically with an rseB disruption. 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 | 256 | R → A: Dramatically increases the basal rate of RseA cleavage. 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 | 256 | R → D: Dramatically increases the basal rate of RseA cleavage. 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 | 320 | D → A: Dramatically increases the basal rate of RseA cleavage. 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 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 ‘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_0000026938 | 1 – 355 | Serine endoprotease DegSAdd BLAST | 355 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AEE3 |
PRoteomics IDEntifications database More...PRIDEi | P0AEE3 |
<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"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN. - Ref.17"Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease."
Wilken C., Kitzing K., Kurzbauer R., Ehrmann M., Clausen T.
Cell 117:483-494(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 43-355 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF TYR-162; PRO-183 AND GLU-227, REACTION MECHANISM, SUBUNIT, ACTIVE SITE. - Ref.18"Structural analysis of DegS, a stress sensor of the bacterial periplasm."
Zeth K.
FEBS Lett. 569:351-358(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 37-354, SUBUNIT, ACTIVE SITE. - Ref.19"Allosteric activation of DegS, a stress sensor PDZ protease."
Sohn J., Grant R.A., Sauer R.T.
Cell 131:572-583(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 27-256 AND MUTANT ALA-178, MUTAGENESIS OF ASP-122; TYR-162; ARG-178; PRO-183; GLU-227; LYS-243; ARG-256 AND ASP-320, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.20"Regulation of the sigmaE stress response by DegS: how the PDZ domain keeps the protease inactive in the resting state and allows integration of different OMP-derived stress signals upon folding stress."
Hasselblatt H., Kurzbauer R., Wilken C., Krojer T., Sawa J., Kurt J., Kirk R., Hasenbein S., Ehrmann M., Clausen T.
Genes Dev. 21:2659-2670(2007) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 43-252 IN COMPLEX WITH ANALOGS SUBSTRATE, FUNCTION AS A SENSOR, FUNCTION AS A PROTEASE, ENZYME REGULATION, BINDING OF PEPTIDE, SUBUNIT, MUTAGENESIS OF ASP-122 AND TYR-162. - Ref.21"OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism."
Sohn J., Grant R.A., Sauer R.T.
Structure 17:1411-1421(2009) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 27-256 OF MUTANT ALA-198 IN COMPLEX WITH ANALOGS SUBSTRATE, MUTAGENESIS OF HIS-198, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT. - Ref.22"Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution."
Sohn J., Grant R.A., Sauer R.T.
J. Biol. Chem. 285:34039-34047(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 27-256 OF MUTANT ALA-162; ALA-178; ALA-191: GLN-198, MUTAGENESIS OF TYR-162; ARG-178; GLN-191 AND HIS-198, ENZYME REGULATION, SUBUNIT, ACTIVE SITE.
<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 | 3 | EBI-1132101,EBI-1132101 | ||
| rseA | P0AFX7 | 7 | EBI-1132101,EBI-1117560 |
<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 | 4261915, 7 interactors |
Database of interacting proteins More...DIPi | DIP-39580N |
Protein interaction database and analysis system More...IntActi | P0AEE3, 3 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3412 |
<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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 39 – 41 | 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 | 48 – 54 | 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 | 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 | 58 – 64 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 67 – 69 | 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 | 76 – 86 | 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 | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 87 – 89 | 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 | 90 – 94 | 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 | 95 – 98 | 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 | 102 – 107 | 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 | 113 – 122 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 123 – 126 | 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 | 127 – 131 | 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 | 153 – 159 | 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 | 161 – 163 | 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 | 166 – 176 | 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 | 11 | |
| <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 | 180 – 182 | 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 | 183 – 185 | 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 | 186 – 188 | 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 | 190 – 192 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 198 – 202 | 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 | 204 – 206 | 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 | 212 – 216 | 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 | 220 – 225 | 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 | 233 – 237 | 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 | 238 – 251 | 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 | 14 | |
| <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 | 261 – 265 | 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 | 271 – 274 | 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 | 276 – 278 | 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 | 282 – 287 | 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 | 289 – 291 | 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 hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 292 – 296 | 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 | 304 – 307 | 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 helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 315 – 323 | 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 | 9 | |
| <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 | 330 – 339 | 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 beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 341 – 347 | 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 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0AEE3 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AEE3 |
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 | P0AEE3 |
<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 | 281 – 326 | PDZPROSITE-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 | 46 |
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 | 259 – 264 | Substrate binding | 6 |
<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.11"OMP peptide signals initiate the envelope-stress response by activating DegS protease via relief of inhibition mediated by its PDZ domain."
Walsh N.P., Alba B.M., Bose B., Gross C.A., Sauer R.T.
Cell 113:61-71(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION AS A SENSOR, FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, BINDING OF PEPTIDES, SUBUNIT, DOMAIN. - Ref.12"Inhibition of regulated proteolysis by RseB."
Cezairliyan B.O., Sauer R.T.
Proc. Natl. Acad. Sci. U.S.A. 104:3771-3776(2007) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN CLEAVAGE OF RSEA, ENZYME REGULATION, DOMAIN.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<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 - Domaini
Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105C0H Bacteria COG0265 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000223641 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AEE3 |
KEGG Orthology (KO) More...KOi | K04691 |
Identification of Orthologs from Complete Genome Data More...OMAi | AHVVINK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AEE3 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001478 PDZ IPR036034 PDZ_sf IPR011783 Pept_S1C_DegS IPR009003 Peptidase_S1_PA IPR001940 Peptidase_S1C |
Pfam protein domain database More...Pfami | View protein in Pfam PF13180 PDZ_2, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00834 PROTEASES2C |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00228 PDZ, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50156 SSF50156, 1 hit SSF50494 SSF50494, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02038 protease_degS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50106 PDZ, 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.
10 20 30 40 50
MFVKLLRSVA IGLIVGAILL VAMPSLRSLN PLSTPQFDST DETPASYNLA
60 70 80 90 100
VRRAAPAVVN VYNRGLNTNS HNQLEIRTLG SGVIMDQRGY IITNKHVIND
110 120 130 140 150
ADQIIVALQD GRVFEALLVG SDSLTDLAVL KINATGGLPT IPINARRVPH
160 170 180 190 200
IGDVVLAIGN PYNLGQTITQ GIISATGRIG LNPTGRQNFL QTDASINHGN
210 220 230 240 250
SGGALVNSLG ELMGINTLSF DKSNDGETPE GIGFAIPFQL ATKIMDKLIR
260 270 280 290 300
DGRVIRGYIG IGGREIAPLH AQGGGIDQLQ GIVVNEVSPD GPAANAGIQV
310 320 330 340 350
NDLIISVDNK PAISALETMD QVAEIRPGSV IPVVVMRDDK QLTLQVTIQE
YPATN
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 | 253 | R → A in M24777 (PubMed:3322223).Curated | 1 | |
| <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 | 307 | V → E in M24777 (PubMed:3322223).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 | U15661 Genomic DNA Translation: AAC43993.1 U32495 Genomic DNA Translation: AAC44006.1 U18997 Genomic DNA Translation: AAA58037.1 U00096 Genomic DNA Translation: AAC76267.1 AP009048 Genomic DNA Translation: BAE77278.1 M24777 Unassigned DNA No translation available. |
Protein sequence database of the Protein Information Resource More...PIRi | JC6052 |
NCBI Reference Sequences More...RefSeqi | NP_417702.1, NC_000913.3 WP_000497723.1, NZ_LN832404.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947865 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3204 eco:b3235 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3493 |
<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 | |
|---|---|---|---|---|---|
| P0AEE3 | Serine endoprotease DegS | 355 | |||
| Protease | 355 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 355 | ||||
| DegS serine endoprotease | 355 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 355 | ||||
| +121 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0AEE3 | Serine endoprotease DegS | 355 | |||
| Protease | 355 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 355 | ||||
| DegS serine endoprotease | 355 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 355 | ||||
| +390 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P0AEE3 | Serine endoprotease DegS | 356 | |||
| Outer membrane-stress sensor serine endopeptidase DegS | 356 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 356 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 356 | ||||
| Outer membrane-stress sensor serine endopeptidase DegS | 356 | ||||
| +1521 | |||||
<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 | U15661 Genomic DNA Translation: AAC43993.1 U32495 Genomic DNA Translation: AAC44006.1 U18997 Genomic DNA Translation: AAA58037.1 U00096 Genomic DNA Translation: AAC76267.1 AP009048 Genomic DNA Translation: BAE77278.1 M24777 Unassigned DNA No translation available. |
Protein sequence database of the Protein Information Resource More...PIRi | JC6052 |
NCBI Reference Sequences More...RefSeqi | NP_417702.1, NC_000913.3 WP_000497723.1, NZ_LN832404.1 |
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 |
| 1SOT | X-ray | 2.30 | A/B/C | 43-355 | [»] | |
| 1SOZ | X-ray | 2.40 | A/B/C | 43-355 | [»] | |
| 1TE0 | X-ray | 2.20 | A/B | 37-354 | [»] | |
| 1VCW | X-ray | 3.05 | A/B/C | 43-355 | [»] | |
| 2QF0 | X-ray | 2.50 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
| 2QF3 | X-ray | 2.04 | A/B/C | 27-256 | [»] | |
| 2QGR | X-ray | 2.70 | A | 27-256 | [»] | |
| 2R3U | X-ray | 2.60 | A/B/C | 43-252 | [»] | |
| 2R3Y | X-ray | 2.50 | A/B/C | 43-355 | [»] | |
| 2RCE | X-ray | 2.35 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
| 3B8J | X-ray | 2.51 | A | 27-256 | [»] | |
| 3GCN | X-ray | 3.00 | A | 27-355 | [»] | |
| 3GCO | X-ray | 2.80 | A | 27-355 | [»] | |
| 3GDS | X-ray | 2.85 | A | 27-355 | [»] | |
| 3GDU | X-ray | 3.00 | A/B/C | 27-355 | [»] | |
| 3GDV | X-ray | 2.49 | A/B/C | 27-355 | [»] | |
| 3LGI | X-ray | 1.65 | A/B/C | 27-256 | [»] | |
| 3LGT | X-ray | 2.68 | A | 27-256 | [»] | |
| 3LGU | X-ray | 2.46 | A | 27-256 | [»] | |
| 3LGV | X-ray | 2.73 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
| 3LGW | X-ray | 2.50 | A | 27-256 | [»] | |
| 3LGY | X-ray | 2.70 | A | 27-256 | [»] | |
| 3LH1 | X-ray | 2.51 | A | 27-256 | [»] | |
| 3LH3 | X-ray | 2.35 | A/B/C/D/E/F/G/H/I | 27-256 | [»] | |
| 4RQY | X-ray | 2.20 | A/B | 37-355 | [»] | |
| 4RQZ | X-ray | 2.40 | A/B/C | 43-355 | [»] | |
| 4RR0 | X-ray | 3.05 | A/B/C | 43-355 | [»] | |
| 4RR1 | X-ray | 2.30 | A/B/C | 43-355 | [»] | |
| 6EW9 | X-ray | 2.20 | A/B/C | 43-355 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P0AEE3 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P0AEE3 | |||||
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 | 4261915, 7 interactors |
Database of interacting proteins More...DIPi | DIP-39580N |
Protein interaction database and analysis system More...IntActi | P0AEE3, 3 interactors |
STRING: functional protein association networks More...STRINGi | 316385.ECDH10B_3412 |
Protein family/group databases
MEROPS protease database More...MEROPSi | S01.275 |
Proteomic databases
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P0AEE3 |
PRoteomics IDEntifications database More...PRIDEi | P0AEE3 |
Protocols and materials databases
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAC76267; AAC76267; b3235 BAE77278; BAE77278; BAE77278 |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 947865 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | ecj:JW3204 eco:b3235 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|1411691.4.peg.3493 |
Organism-specific databases
EchoBASE - an integrated post-genomic database for E. coli More...EchoBASEi | EB1605 |
Escherichia coli strain K12 genome database More...EcoGenei | EG11652 degS |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | ENOG4105C0H Bacteria COG0265 LUCA |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000223641 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P0AEE3 |
KEGG Orthology (KO) More...KOi | K04691 |
Identification of Orthologs from Complete Genome Data More...OMAi | AHVVINK |
Database for complete collections of gene phylogenies More...PhylomeDBi | P0AEE3 |
Enzyme and pathway databases
BioCyc Collection of Pathway/Genome Databases More...BioCyci | EcoCyc:EG11652-MONOMER MetaCyc:EG11652-MONOMER |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P0AEE3 |
Protein Ontology More...PROi | PR:P0AEE3 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001478 PDZ IPR036034 PDZ_sf IPR011783 Pept_S1C_DegS IPR009003 Peptidase_S1_PA IPR001940 Peptidase_S1C |
Pfam protein domain database More...Pfami | View protein in Pfam PF13180 PDZ_2, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00834 PROTEASES2C |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00228 PDZ, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF50156 SSF50156, 1 hit SSF50494 SSF50494, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02038 protease_degS, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS50106 PDZ, 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 | DEGS_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 | P0AEE3Primary (citable) accession number: P0AEE3 Secondary accession number(s): P31137, Q2M8X8 | |
| <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: | December 6, 2005 |
| Last sequence update: | December 6, 2005 | |
| Last modified: | June 20, 2018 | |
| This is version 105 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, 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 - Peptidase families
Classification of peptidase families and list of entries - SIMILARITY comments
Index of protein domains and families
