Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O05689 (CRP_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 96. 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:PM1157
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length209 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 – 209209cAMP-activated global transcriptional regulator CRP
PRO_0000100149

Regions

Domain137 – 20973HTH crp-type
Nucleotide binding56 – 627cAMP 1 By similarity
Nucleotide binding71 – 733cAMP 1 By similarity
Nucleotide binding82 – 832cAMP 1 By similarity
Nucleotide binding127 – 1282cAMP 1 By similarity
Nucleotide binding135 – 1362cAMP 2 By similarity
Nucleotide binding170 – 18011cAMP 2 By similarity
DNA binding179 – 1857H-T-H motif By similarity
Region19 – 213Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity
Region52 – 587Activating region 3 (AR3); probably contacts sigma-70 (RpoD) By similarity
Region153 – 16210Activating region 1 (AR1); probably contacts the C-terminus of RpoA By similarity

Sites

Site961Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity
Site1011Activating region 2 (AR2); probably contacts the N-terminus of RpoA By similarity

Amino acid modifications

Modified residue1001N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
O05689 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 2E6A60E75F9CEF07

FASTA20923,541
        10         20         30         40         50         60 
MQTTPSIDPT LEWFLSHCHI HKYPSKSTLI HAGEKAETLY YLIKGSVAVL VKDEDGKEMI 

        70         80         90        100        110        120 
LTYLSQGDFF GEAGLFEEGQ LRSAWIKAKS PCEIAEISYK KFRQLIQVNP DILMHLSAQL 

       130        140        150        160        170        180 
ARRLQNTSRQ VSNLAFLDVT GRIAQTLLNL AKMPEAMTHP DGMQIKITRQ EIGQMVGCSR 

       190        200 
ETVGRILKML EDQHLISAHG KTIVVYGTR 

« Hide

References

« Hide 'large scale' references
[1]"Isolation and characterization of crp mutants in Pasteurella multocida."
Roland K.L., Mukkur T.K., Ball T.K.
Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U95380 Genomic DNA. Translation: AAB53064.1.
AE004439 Genomic DNA. Translation: AAK03241.1.
RefSeqNP_246094.1. NC_002663.1.

3D structure databases

ProteinModelPortalO05689.
SMRO05689. Positions 8-209.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM1157.

Proteomic databases

PRIDEO05689.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK03241; AAK03241; PM1157.
GeneID1244504.
KEGGpmu:PM1157.
PATRIC22871567. VBIPasMul88067_1168.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0664.
HOGENOMHOG000250565.
KOK10914.
OMASETHPEF.
OrthoDBEOG69GZGV.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-1207-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_PASMU
AccessionPrimary (citable) accession number: O05689
Entry history
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: July 1, 1997
Last modified: May 14, 2014
This is version 96 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