Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P0ACJ8 (CRP_ECOLI)

Entry version 129 (11 Dec 2019)
Sequence version 1 (21 Jul 1986)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score:

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>

<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

A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding (to consensus sequence 5'-AAATGTGATCTAGATCACATTT-3') to directly regulate the transcription of about 300 genes in about 200 operons and indirectly regulate the expression of about half the genome. There are 3 classes of CRP promoters; class I promoters have a single CRP-binding site upstream of the RNA polymerase (RNAP)-binding site, whereas in class II promoters the single CRP- and RNAP-binding site overlap, CRP making multiple contacts with RNAP. Class III promoters require multiple activator molecules, including at least one CRP dimer. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA (about 87 degrees), bringing upstream promoter elements into contact with RNAP. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. High levels of active CRP are detrimental to growth (PubMed:16260780). Plays a major role in carbon catabolite repression (CCR). CCR involves cAMP, adenylate cyclase (cyaA), CRP and the EIIA-Glc component of the PTS (crr). In the presence of glucose EIIA-Glc is dephosphorylated, and does not activate adenylate cyclase, leading to reduced cAMP and thus decreased CRP activity. Also plays a role in many other processes (see PubMed:22573269).10 Publications

Miscellaneous

Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

In the apo-form the DNA-binding helices form a rigid body in which their DNA recognitions helices are buried. cAMP binding causes a coil-to helix transition, stabilizing the active DNA binding conformation by reorienting and elongating these helices, which precludes a return to the inactive state.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei97Activating region 2 (AR2); probably contacts the N-terminus of RpoA1
Sitei102Activating region 2 (AR2); probably contacts the N-terminus of RpoA1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei129cAMP6 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi57 – 63cAMP 16 Publications7
Nucleotide bindingi72 – 74cAMP 16 Publications3
Nucleotide bindingi83 – 84cAMP 16 Publications2
Nucleotide bindingi128 – 129cAMP 16 Publications2
Nucleotide bindingi136 – 137cAMP 26 Publications2
Nucleotide bindingi171 – 181cAMP 26 PublicationsAdd BLAST11
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi180 – 186H-T-H motifPROSITE-ProRule annotation7

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandcAMP, cAMP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		EcoCyc:PD00257
ECOL316407:JW5702-MONOMER

<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 CRP
Alternative 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>OrganismiEscherichia 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 identifieri83333 [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 lineageiBacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia ›
<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
  • UP000000318 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

<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

GO - Cellular componenti

Complete GO annotation on QuickGO ...

<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

Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant.3 Publications

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Mutagenesisi20H → A, L or Y: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication1
Mutagenesisi22H → A or L: Decreased transcription activation at class II promoters, decreased interaction with RNAP, binds DNA. 1 Publication1
Mutagenesisi53K → N: Increased activation at class II promoters, increased interaction with RNAP. 1 Publication1
Mutagenesisi54 – 56DEE → AAA: 80% reduction in activation of class II promoters; 95% loss when associated with A-59. 1 Publication3
Mutagenesisi59E → A: 45% reduction in activation of class II promoters; 95% loss when associated with AAA-54-56. 2 Publications1
Mutagenesisi59E → G or K: Reduction in activation of class II promoters. 2 Publications1
Mutagenesisi63S → A: Enhanced cAMP-binding, enhanced transcription. 1 Publication1
Mutagenesisi83R → L: Loss of cAMP-binding. 1 Publication1
Mutagenesisi84S → A or K: No modification of cAMP-binding. 1 Publication1
Mutagenesisi97E → A: Increased transcription activation at class II promoters, binds DNA. 1 Publication1
Mutagenesisi102K → E: Disrupts AR2. No activation of class II promoters, decreased interaction with RNAP, binds DNA. 2 Publications1
Mutagenesisi128 – 129TS → 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 Publications2
Mutagenesisi128T → A: No modification of cAMP-binding. 1 Publication1
Mutagenesisi129S → A: Reduced DNA-binding; no modification of cAMP-binding. 2 Publications1
Mutagenesisi139D → L: Some stabilization of an inactive (apo-) form. Decreased affinity for DNA, normal subunit association. 3 Publications1
Mutagenesisi157A → D or P: Decreased transcription activation (6-29%), binds DNA. 2 Publications1
Mutagenesisi159T → A, I, N, S or V: Decreased transcription activation (15-87%) at class I and II promoters, binds DNA. 3 Publications1
Mutagenesisi160H → 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 Publications1
Mutagenesisi163G → A, C, D, R, S or V: Decreased transcription activation (2-62%) at class I and II promoters, binds DNA. 3 Publications1
Mutagenesisi181R → K: Suppresses DNA-binding. 1 Publication1
Mutagenesisi181R → L: Suppresses DNA-binding. 1 Publication1
Mutagenesisi186R → K: No modification of DNA-binding. 1 Publication1
Mutagenesisi186R → L: Marginally reduced DNA-binding. 1 Publication1

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 keyPosition(s)DescriptionActionsGraphical viewLength
<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 methionineiRemoved1 Publication
<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_00001001442 – 210cAMP-activated global transcriptional regulator CRPAdd BLAST209

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei101N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P0ACJ8

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		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

Constitutively expressed, levels decrease in stationary phase; more strongly induced in an rnlA deletion mutant, levels remain high even in stationary phase (at protein level). Both positively (PubMed:1328816) and negatively autoregulated (PubMed:6297782).3 Publications

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

Homodimer, which upon binding cAMP is able to bind DNA. AR1 of the upstream subunit binds to the C-terminus of RNAP subunit RpoA, AR2 of the downstream subunit binds to the N-terminus of RpoA while AR3 binds to sigma-70 (RpoD).

14 Publications

<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

Show more details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		4262928, 15 interactors
852178, 31 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		511145.b3357

<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

1210
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P0ACJ8

Database of comparative protein structure models

More...ModBasei		Search...

Protein Data Bank in Europe - Knowledge Base

More...PDBe-KBi		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 keyPosition(s)DescriptionActionsGraphical viewLength
<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>Domaini138 – 210HTH crp-typePROSITE-ProRule annotationAdd BLAST73

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Regioni20 – 22Activating region 2 (AR2); probably contacts the N-terminus of RpoA3
Regioni53 – 59Activating region 3 (AR3); probably contacts sigma-70 (RpoD)7
Regioni154 – 163Activating region 1 (AR1); probably contacts the C-terminus of RpoA10

<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

The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound.2 Publications

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

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
PF13545 HTH_Crp_2, 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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

P0ACJ8-1 [UniParc]FASTAAdd to basket
« Hide
        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
Length:210
Mass (Da):23,640
Last modified:July 21, 1986 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDCBC24FA46C61B3D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 conflicti29T → K in BAE77933 (PubMed:16738553).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links 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_STEB01000004.1

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

<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:
EMBLi
GenBanki
DDBJi
Links 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
PIRiA93416 QRECC
RefSeqiNP_417816.1, NC_000913.3
WP_000242755.1, NZ_STEB01000004.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1CGPX-ray3.00A/B2-206[»]
1G6NX-ray2.10A/B1-210[»]
1HW5X-ray1.82A/B1-210[»]
1I5ZX-ray1.90A/B2-210[»]
1I6XX-ray2.20A/B2-210[»]
1J59X-ray2.50A/B2-210[»]
1LB2X-ray3.10A2-210[»]
1O3QX-ray3.00A9-208[»]
1O3RX-ray3.00A9-208[»]
1O3SX-ray3.00A9-208[»]
1O3TX-ray2.80A/B9-208[»]
1RUNX-ray2.70A/B2-210[»]
1RUOX-ray2.70A/B2-210[»]
1ZRCX-ray2.80A/B2-210[»]
1ZRDX-ray2.80A/B2-210[»]
1ZREX-ray2.80A/B2-210[»]
1ZRFX-ray2.10A/B2-210[»]
2CGPX-ray2.20A1-210[»]
2GAPmodel-A/B2-209[»]
2GZWX-ray2.21A/B/C/D2-210[»]
2WC2NMR-A/B2-210[»]
3FWEX-ray2.30A/B1-210[»]
3HIFX-ray3.59A/B/C/D/E/F1-210[»]
3IYDelectron microscopy-G/H2-210[»]
3KCCX-ray1.66A/B1-210[»]
3N4MX-ray2.99A2-210[»]
3QOPX-ray1.96A/B1-210[»]
3RDIX-ray2.95A/B1-210[»]
3ROUX-ray2.10A/B1-210[»]
3RPQX-ray2.61A/B1-210[»]
3RYPX-ray1.60A/B1-210[»]
3RYRX-ray2.70A/B1-210[»]
4BH9NMR-A2-210[»]
4BHPNMR-A2-210[»]
4FT8X-ray1.97A/B2-210[»]
4HZFX-ray1.48A/B1-210[»]
4I01X-ray2.30A/B1-210[»]
4I02X-ray1.75A/B/C/D/E/F1-210[»]
4I09X-ray2.05A/B1-210[»]
4I0AX-ray2.20A/B1-210[»]
4I0BX-ray1.50A/B1-210[»]
4R8HX-ray1.46A/B1-210[»]
5CIZX-ray5.01A2-210[»]
SMRiP0ACJ8
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi4262928, 15 interactors
852178, 31 interactors
DIPiDIP-29232N
IntActiP0ACJ8, 42 interactors
MINTiP0ACJ8
STRINGi511145.b3357

Chemistry databases

DrugBankiDB02527 Cyclic adenosine monophosphate

PTM databases

iPTMnetiP0ACJ8

Proteomic databases

EPDiP0ACJ8
jPOSTiP0ACJ8
PaxDbiP0ACJ8
PRIDEiP0ACJ8

Genome annotation databases

EnsemblBacteriaiAAC76382; AAC76382; b3357
BAE77933; BAE77933; BAE77933
GeneIDi33939152
947867
KEGGiecj:JW5702
eco:b3357
PATRICifig|1411691.4.peg.3373

Organism-specific databases

EchoBASE - an integrated post-genomic database for E. coli

More...EchoBASEi		EB0162

Phylogenomic databases

eggNOGiCOG0664 LUCA
HOGENOMiHOG000250565
InParanoidiP0ACJ8
KOiK10914
PhylomeDBiP0ACJ8

Enzyme and pathway databases

BioCyciEcoCyc:PD00257
ECOL316407:JW5702-MONOMER

Miscellaneous databases

EvolutionaryTraceiP0ACJ8

Protein Ontology

More...PROi		PR:P0ACJ8

Gene expression databases

CollecTFiEXPREG_00000850

Family and domain databases

CDDicd00038 CAP_ED, 1 hit
Gene3Di1.10.10.10, 1 hit
2.60.120.10, 1 hit
InterProiView 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
PfamiView protein in Pfam
PF00027 cNMP_binding, 1 hit
PF13545 HTH_Crp_2, 1 hit
PRINTSiPR00034 HTHCRP
SMARTiView protein in SMART
SM00100 cNMP, 1 hit
SM00419 HTH_CRP, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
SSF51206 SSF51206, 1 hit
PROSITEiView 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...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		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 nameiCRP_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>AccessioniPrimary (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 historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: December 11, 2019
This is version 129 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 statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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

Keywords - Technical termi

3D-structure, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again