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P0ACJ9 (CRP_ECOL6) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Gene names
Name:crp
Ordered Locus Names:c4132
OrganismEscherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier199310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

A global transcription regulator. Complexes with cyclic AMP (cAMP) which allosterically activates DNA binding to regulate transcription. It can act as an activator, repressor, coactivator or corepressor. Induces a severe bend in DNA. Acts as a negative regulator of its own synthesis as well as for adenylate cyclase (cyaA), which generates cAMP. Plays a major role in carbon catabolite repression (CCR) By similarity.

Subunit structure

Homodimer, which upon binding cAMP is able to bind DNA. Binds the N- and C-terminus of RNA polymerase subunit RpoA and sigma-70 (RpoD) By similarity.

Domain

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

Sequence similarities

Contains 1 cyclic nucleotide-binding domain.

Contains 1 HTH crp-type DNA-binding domain.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210cAMP-activated global transcriptional regulator CRP
PRO_0000100146

Regions

Domain138 – 21073HTH crp-type
Nucleotide binding57 – 637cAMP 1 By similarity
Nucleotide binding72 – 743cAMP 1 By similarity
Nucleotide binding83 – 842cAMP 1 By similarity
Nucleotide binding128 – 1292cAMP 1 By similarity
Nucleotide binding136 – 1372cAMP 2 By similarity
Nucleotide binding171 – 18111cAMP 2 By similarity
DNA binding180 – 1867H-T-H motif By similarity
Region20 – 223Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity
Region53 – 597Activating region 3 (AR3); probably contacts sigma-70 (RpoD) By similarity
Region154 – 16310Activating region 1 (AR1); probably contacts the C-terminus of RpoA By similarity

Sites

Site971Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity
Site1021Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity

Amino acid modifications

Modified residue1011N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0ACJ9 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: DCBC24FA46C61B3D

FASTA21023,640
        10         20         30         40         50         60 
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM 

        70         80         90        100        110        120 
ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY KKFRQLIQVN PDILMRLSAQ 

       130        140        150        160        170        180 
MARRLQVTSE KVGNLAFLDV TGRIAQTLLN LAKQPDAMTH PDGMQIKITR QEIGQIVGCS 

       190        200        210 
RETVGRILKM LEDQNLISAH GKTIVVYGTR 

« Hide

References

[1]"Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli."
Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R.
Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CFT073 / ATCC 700928 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE014075 Genomic DNA. Translation: AAN82570.1.
RefSeqNP_755996.1. NC_004431.1.

3D structure databases

ProteinModelPortalP0ACJ9.
SMRP0ACJ9. Positions 9-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING199310.c4132.

Proteomic databases

PRIDEP0ACJ9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAN82570; AAN82570; c4132.
GeneID1036667.
KEGGecc:c4132.
PATRIC18286014. VBIEscCol75197_3883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000250565.
KOK10914.
OMALGSQMAE.
OrthoDBEOG69GZGV.

Enzyme and pathway databases

BioCycECOL199310:C4132-MONOMER.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProIPR018490. 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.
[Graphical view]
PfamPF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]
PRINTSPR00034. HTHCRP.
SMARTSM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]
SUPFAMSSF51206. SSF51206. 1 hit.
PROSITEPS00888. 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.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCRP_ECOL6
AccessionPrimary (citable) accession number: P0ACJ9
Secondary accession number(s): P03020
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: May 14, 2014
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families