UniProt Accession

 CRP_ECOLI; P0ACJ8; P03020; Q2M723 

Genbank Protein ID

 J01598; U18997; U00096; AP009048 

Genbank Nucleotide ID

 AAA23601.1; AAA58154.1; AAC76382.1; BAE77933.1 

Protein Name

 cAMP receptor protein 

Protein Synonyms/Alias

 Crp; Catabolite gene activator; CAP; cAMP regulatory protein 

Gene Name

 crp 

Gene Synonyms/Alias

 cap; csm; b3357; JW5702 

Created Date

 July 27, 2013 

Organism

 Escherichia coli (strain K12) 

NCBI Taxa ID

 83333 

Lysine Modification

Position	Peptide	Type	References
5	***MVLGKPQTDPTL	acetylation	[1]
23	LSHCHIHKYPSKSTL	acetylation	[1]
27	HIHKYPSKSTLIHQG	acetylation	[1]
36	TLIHQGEKAETLYYI	acetylation	[1]
53	GSVAVLIKDEEGKEM	acetylation	[1, 2]
90	RSAWVRAKTACEVAE	acetylation	[1]
101	EVAEISYKKFRQLIQ	acetylation	[1, 3, 4]
102	VAEISYKKFRQLIQV	acetylation	[1]
131	RLQVTSEKVGNLAFL	acetylation	[1]
153	QTLLNLAKQPDAMTH	acetylation	[1]
167	HPDGMQIKITRQEIG	acetylation	[1, 4]
189	ETVGRILKMLEDQNL	acetylation	[1]
202	NLISAHGKTIVVYGT	acetylation	[1]

Reference

 [1] Acetyl-Phosphate Is a Critical Determinant of Lysine Acetylation in E. coli.
 Weinert BT, Iesmantavicius V, Wagner SA, Schölz C, Gummesson B, Beli P, Nyström T, Choudhary C.
 Mol Cell. 2013 Jul 25;51(2):265-72. [PMID: 23830618]
 [2] The diversity of lysine-acetylated proteins in Escherichia coli.
 Yu BJ, Kim JA, Moon JH, Ryu SE, Pan JG.
 J Microbiol Biotechnol. 2008 Sep;18(9):1529-36. [PMID: 18852508]
 [3] Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli.
 Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y.
 Mol Cell Proteomics. 2009 Feb;8(2):215-25. [PMID: 18723842]
 [4] Comprehensive profiling of protein lysine acetylation in Escherichia coli.
 Zhang K, Zheng S, Yang JS, Chen Y, Cheng Z.
 J Proteome Res. 2013 Feb 1;12(2):844-51. [PMID: 23294111] 

Functional Description

 This protein complexes with cyclic AMP and binds to specific DNA sites near the promoter to regulate the transcription of several catabolite-sensitive operons. The protein induces a severe bend in the DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. 

Sequence Annotation

 DOMAIN 138 210 HTH crp-type.
 NP_BIND 10 133 cAMP.
 DNA_BIND 170 189 H-T-H motif.
 BINDING 129 129 cAMP.
 MOD_RES 101 101 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Activator; cAMP; cAMP-binding; Complete proteome; Direct protein sequencing; DNA-binding; Nucleotide-binding; Reference proteome; Repressor; Transcription; Transcription regulation. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 210 AA 

Protein Sequence

Gene Ontology

 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; IEA:InterPro.
 GO:0045013; P:carbon catabolite repression of transcription; IMP:EcoCyc.
 GO:0045893; P:positive regulation of transcription, DNA-dependent; IDA:EcoliWiki.
 GO:0006351; P:transcription, DNA-dependent; IDA:EcoCyc. 

Interpro

 IPR018490; cNMP-bd-like.
 IPR018488; cNMP-bd_CS.
 IPR000595; cNMP-bd_dom.
 IPR012318; HTH_CRP_2.
 IPR014710; RmlC-like_jellyroll.
 IPR001808; Tscrpt_reg_HTH_Crp.
 IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
 IPR011991; WHTH_DNA-bd_dom. 

Pfam

 PF00027; cNMP_binding
 PF00325; Crp 

SMART

 SM00100; cNMP
 SM00419; HTH_CRP 

PROSITE

 PS00888; CNMP_BINDING_1
 PS00889; CNMP_BINDING_2
 PS50042; CNMP_BINDING_3
 PS00042; HTH_CRP_1
 PS51063; HTH_CRP_2 

PRINTS

 PR00034; HTHCRP.