{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P0ACJ8","secondaryAccessions":["P03020","Q2M723"],"uniProtkbId":"CRP_ECOLI","entryAudit":{"firstPublicDate":"1986-07-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1986-07-21","entryVersion":159,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Escherichia coli (strain K12)","taxonId":83333,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Enterobacterales","Enterobacteriaceae","Escherichia"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"DNA-binding transcriptional dual regulator CRP"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8392187"}],"value":"Catabolite activator protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8392187"}],"value":"CAP"}]},{"fullName":{"value":"Catabolite gene activator"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6280140"}],"value":"cAMP receptor protein"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"6280140"}],"value":"CRP"}]},{"fullName":{"value":"cAMP regulatory protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"cAMP-activated global transcriptional regulator CRP"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"164435"}],"value":"crp"},"synonyms":[{"value":"cap"},{"value":"csm"}],"orderedLocusNames":[{"value":"b3357"},{"value":"JW5702"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10860739"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10860740"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14990258"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15520470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16260780"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16301522"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2982847"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7966284"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8392187"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8978616"}],"value":"A global transcription regulator, which plays a major role in carbon catabolite repression (CCR) as well as other processes. Binds 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. CRP 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). In CCR it prevents expression of genes involved in catabolism of nonpreferred carbon sources when glucose is present. 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. When glucose is absent cAMP binds to CRP, up-regulating expression of genes involved in the consumption of non-glucose carbon sources. Also plays a role in many other processes (see PubMed:22573269)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21292161"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2454912"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35239441"}],"value":"Among the targets of CRP is the spf gene which encodes the dual-function sRNA Spot 42; spf expression is repressed by CRP (PubMed:2454912). Spot 42 base pairs with and represses expression from a number of mRNAs encoding proteins involved in the uptake and catabolism of nonpreferred carbon sources. CRP and Spot 42 coregulate at least 14 operons involved in cellular metabolism, forming a coherent feedforward loop (PubMed:21292161). Interaction with SpfP, encoded within the Spot 42 RNA, reinforces this feedforward loop (PubMed:35239441)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14990258"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"19439203"}],"value":"Some mutants (called CRP* or CAP*) are constitutively active even in the absence of cAMP (PubMed:19439203). Strain DHKD, a CAP* mutant, confers cAMP-independent expression and relief of catabolite repression of beta-galactosidase and tryptophanase synthesis (PubMed:14990258). Strain CA8404, another CAP* mutant, confers cAMP-independent expression and relief of catabolite repression of beta-galactosidase but not of tryptophanase synthesis (PubMed:14990258)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19359484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19805344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35239441"}],"value":"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 (PubMed:19359484, PubMed:19805344). Interaction with SpfP blocks activation of some, but not all, CRP-dependent genes (PubMed:35239441)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11124031"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12202833"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1646077"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1653449"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19359484"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19805344"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19903881"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2828639"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2839152"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"35239441"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6286624"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8757802"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8978616"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9096308"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.45"}],"value":"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) (PubMed:11124031, PubMed:12202833, PubMed:1646077, PubMed:1653449, PubMed:19359484, PubMed:19805344, PubMed:19903881, PubMed:2828639, PubMed:2839152, PubMed:6286624, PubMed:8757802, PubMed:8978616, PubMed:9096308, Ref.45). Interacts with SpfP (PubMed:35239441)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"P0ACJ8","intActId":"EBI-547513"},"interactantTwo":{"uniProtKBAccession":"P0ACJ8","geneName":"crp","intActId":"EBI-547513"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACJ8","intActId":"EBI-547513"},"interactantTwo":{"uniProtKBAccession":"P0AFG0","geneName":"nusG","intActId":"EBI-369628"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACJ8","intActId":"EBI-547513"},"interactantTwo":{"uniProtKBAccession":"P23862","geneName":"priC","intActId":"EBI-1117383"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACJ8","intActId":"EBI-547513"},"interactantTwo":{"uniProtKBAccession":"P0A7K2","geneName":"rplL","intActId":"EBI-543702"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"P0ACJ8","intActId":"EBI-547513"},"interactantTwo":{"uniProtKBAccession":"P0A8E5","geneName":"yacL","intActId":"EBI-554965"},"numberOfExperiments":4,"organismDiffer":false}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1328816"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19019153"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6297782"}],"value":"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)"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2828639"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"6286624"}],"value":"The N-terminal domain binds cAMP and is responsible for homodimerization, while the C-terminal domain binds DNA when cAMP is bound"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15520470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"164435"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19019153"}],"value":"Not essential (on rich medium), greatly increased levels of cAMP. Eliminates the NaCl sensitivity of an rnlA deletion mutant"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"9096308"}],"value":"Binds 2 cAMP; cAMP 1 is in the anti conformation, while cAMP 2 is in the syn conformation"}],"commentType":"MISCELLANEOUS"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17895580"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"DNA-binding transcriptional dual regulator CRP","featureId":"PRO_0000100144"},{"type":"Domain","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"HTH crp-type","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00387"}]},{"type":"DNA binding","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"H-T-H motif","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00387"}]},{"type":"Region","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Activating region 2 (AR2); 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