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P0A2T6 (CRP_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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
Synonyms:cap
Ordered Locus Names:STM3466
OrganismSalmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) [Reference proteome] [HAMAP]
Taxonomic identifier99287 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length210 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 210210cAMP-activated global transcriptional regulator CRP
PRO_0000100150

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

Experimental info

Mutagenesis1311K → Q or T in acr-4 and acr-3 respectively; higher levels of cAMP synthesis. Ref.2
Sequence conflict401L → S in AAA62414. Ref.2
Sequence conflict1191S → A in AAA62414. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P0A2T6 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: C54244E974D53A0F

FASTA21023,656
        10         20         30         40         50         60 
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM 

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

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

       190        200        210 
RETVGRILKM LEDQNLISAH GKTIVVYGTR 

« Hide

References

« Hide 'large scale' references
[1]"crp genes of Shigella flexneri, Salmonella typhimurium, and Escherichia coli."
Cossart P., Groisman E.A., Serre M.-C., Casadaban M.J., Gicquel-Sanzey B.
J. Bacteriol. 167:639-646(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[2]"Cloning and DNA sequence analysis of the wild-type and mutant cyclic AMP receptor protein genes from Salmonella typhimurium."
Schroeder C.J., Dobrogosz W.J.
J. Bacteriol. 167:616-622(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], MUTAGENESIS OF LYS-131.
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M13773 Genomic DNA. Translation: AAA27039.1.
M13770 Genomic DNA. Translation: AAA62414.1.
AE006468 Genomic DNA. Translation: AAL22328.1.
PIRA26049.
RefSeqNP_462369.1. NC_003197.1.

3D structure databases

ProteinModelPortalP0A2T6.
SMRP0A2T6. Positions 2-208.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING99287.STM3466.

Proteomic databases

PaxDbP0A2T6.
PRIDEP0A2T6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL22328; AAL22328; STM3466.
GeneID1254989.
KEGGstm:STM3466.
PATRIC32385731. VBISalEnt20916_3663.

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000250565.
KOK10914.
OMADQLYFIV.
OrthoDBEOG69GZGV.
ProtClustDBPRK11753.

Enzyme and pathway databases

BioCycSENT99287:GCTI-3488-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_SALTY
AccessionPrimary (citable) accession number: P0A2T6
Secondary accession number(s): P06170, P29282
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: February 19, 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