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O05689

- CRP_PASMU

UniProt

O05689 - CRP_PASMU

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Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Pasteurella multocida (strain Pm70)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

Functioni

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).By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei96 – 961Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity
Sitei101 – 1011Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 627cAMP 1By similarity
Nucleotide bindingi71 – 733cAMP 1By similarity
Nucleotide bindingi82 – 832cAMP 1By similarity
Nucleotide bindingi127 – 1282cAMP 1By similarity
Nucleotide bindingi135 – 1362cAMP 2By similarity
Nucleotide bindingi170 – 18011cAMP 2By similarityAdd
BLAST
DNA bindingi179 – 1857H-T-H motifPROSITE-ProRule annotation

GO - Molecular functioni

  1. cAMP binding Source: UniProtKB-KW
  2. DNA binding Source: UniProtKB-KW
  3. sequence-specific DNA binding transcription factor activity Source: InterPro

GO - Biological processi

  1. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

cAMP, cAMP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-1207-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:crp
Ordered Locus Names:PM1157
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

Subcellular locationi

GO - Cellular componenti

  1. intracellular Source: InterPro
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209cAMP-activated global transcriptional regulator CRPPRO_0000100149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiO05689.

Interactioni

Subunit structurei

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).By similarity

Protein-protein interaction databases

STRINGi272843.PM1157.

Structurei

3D structure databases

ProteinModelPortaliO05689.
SMRiO05689. Positions 8-209.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini137 – 20973HTH crp-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni19 – 213Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity
Regioni52 – 587Activating region 3 (AR3); probably contacts sigma-70 (RpoD)By similarity
Regioni153 – 16210Activating region 1 (AR1); probably contacts the C-terminus of RpoABy similarity

Domaini

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 similaritiesi

Contains 1 cyclic nucleotide-binding domain.PROSITE-ProRule annotation
Contains 1 HTH crp-type DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000250565.
KOiK10914.
OMAiSETHPEF.
OrthoDBiEOG69GZGV.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProiIPR018490. 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]
PfamiPF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view]
PRINTSiPR00034. HTHCRP.
SMARTiSM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 1 hit.
PROSITEiPS00888. 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]

Sequencei

Sequence statusi: Complete.

O05689-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQTTPSIDPT LEWFLSHCHI HKYPSKSTLI HAGEKAETLY YLIKGSVAVL
60 70 80 90 100
VKDEDGKEMI LTYLSQGDFF GEAGLFEEGQ LRSAWIKAKS PCEIAEISYK
110 120 130 140 150
KFRQLIQVNP DILMHLSAQL ARRLQNTSRQ VSNLAFLDVT GRIAQTLLNL
160 170 180 190 200
AKMPEAMTHP DGMQIKITRQ EIGQMVGCSR ETVGRILKML EDQHLISAHG

KTIVVYGTR
Length:209
Mass (Da):23,541
Last modified:July 1, 1997 - v1
Checksum:i2E6A60E75F9CEF07
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95380 Genomic DNA. Translation: AAB53064.1.
AE004439 Genomic DNA. Translation: AAK03241.1.
RefSeqiNP_246094.1. NC_002663.1.
WP_010907050.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK03241; AAK03241; PM1157.
GeneIDi1244504.
KEGGipmu:PM1157.
PATRICi22871567. VBIPasMul88067_1168.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U95380 Genomic DNA. Translation: AAB53064.1 .
AE004439 Genomic DNA. Translation: AAK03241.1 .
RefSeqi NP_246094.1. NC_002663.1.
WP_010907050.1. NC_002663.1.

3D structure databases

ProteinModelPortali O05689.
SMRi O05689. Positions 8-209.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 272843.PM1157.

Proteomic databases

PRIDEi O05689.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK03241 ; AAK03241 ; PM1157 .
GeneIDi 1244504.
KEGGi pmu:PM1157.
PATRICi 22871567. VBIPasMul88067_1168.

Phylogenomic databases

eggNOGi COG0664.
HOGENOMi HOG000250565.
KOi K10914.
OMAi SETHPEF.
OrthoDBi EOG69GZGV.

Enzyme and pathway databases

BioCyci PMUL272843:GC8W-1207-MONOMER.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
2.60.120.10. 1 hit.
InterProi 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.
[Graphical view ]
Pfami PF00027. cNMP_binding. 1 hit.
PF00325. Crp. 1 hit.
[Graphical view ]
PRINTSi PR00034. HTHCRP.
SMARTi SM00100. cNMP. 1 hit.
SM00419. HTH_CRP. 1 hit.
[Graphical view ]
SUPFAMi SSF51206. SSF51206. 1 hit.
PROSITEi PS00888. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pm70.

Entry informationi

Entry nameiCRP_PASMU
AccessioniPrimary (citable) accession number: O05689
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: July 1, 1997
Last modified: October 1, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3