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P0ACK0

- CRP_ECO57

UniProt

P0ACK0 - CRP_ECO57

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Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Escherichia coli O157:H7
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
Sitei97 – 971Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity
Sitei102 – 1021Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi57 – 637cAMP 1By similarity
Nucleotide bindingi72 – 743cAMP 1By similarity
Nucleotide bindingi83 – 842cAMP 1By similarity
Nucleotide bindingi128 – 1292cAMP 1By similarity
Nucleotide bindingi136 – 1372cAMP 2By similarity
Nucleotide bindingi171 – 18111cAMP 2By similarityAdd
BLAST
DNA bindingi180 – 1867H-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

BioCyciECOL386585:GJFA-4178-MONOMER.
ECOO157:CRP-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:Z4718, ECs4208
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

Subcellular locationi

GO - Cellular componenti

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210cAMP-activated global transcriptional regulator CRPPRO_0000100145Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei101 – 1011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0ACK0.

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

MINTiMINT-1249633.
STRINGi155864.Z4718.

Structurei

3D structure databases

ProteinModelPortaliP0ACK0.
SMRiP0ACK0. Positions 9-208.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ACK0.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini138 – 21073HTH crp-typePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 223Activating region 2 (AR2); probably contacts the N-terminus of RpoABy similarity
Regioni53 – 597Activating region 3 (AR3); probably contacts sigma-70 (RpoD)By similarity
Regioni154 – 16310Activating 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.

P0ACK0-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV
60 70 80 90 100
LIKDEEGKEM ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY
110 120 130 140 150
KKFRQLIQVN PDILMRLSAQ MARRLQVTSE KVGNLAFLDV TGRIAQTLLN
160 170 180 190 200
LAKQPDAMTH PDGMQIKITR QEIGQIVGCS RETVGRILKM LEDQNLISAH
210
GKTIVVYGTR
Length:210
Mass (Da):23,640
Last modified:July 21, 1986 - v1
Checksum:iDCBC24FA46C61B3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG58465.1.
BA000007 Genomic DNA. Translation: BAB37631.1.
PIRiE86000.
H91154.
RefSeqiNP_289905.1. NC_002655.2.
NP_312235.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG58465; AAG58465; Z4718.
BAB37631; BAB37631; BAB37631.
GeneIDi915936.
958797.
KEGGiece:Z4718.
ecs:ECs4208.
PATRICi18357966. VBIEscCol44059_4150.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA. Translation: AAG58465.1 .
BA000007 Genomic DNA. Translation: BAB37631.1 .
PIRi E86000.
H91154.
RefSeqi NP_289905.1. NC_002655.2.
NP_312235.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0ACK0.
SMRi P0ACK0. Positions 9-208.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1249633.
STRINGi 155864.Z4718.

Proteomic databases

PRIDEi P0ACK0.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG58465 ; AAG58465 ; Z4718 .
BAB37631 ; BAB37631 ; BAB37631 .
GeneIDi 915936.
958797.
KEGGi ece:Z4718.
ecs:ECs4208.
PATRICi 18357966. VBIEscCol44059_4150.

Phylogenomic databases

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

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-4178-MONOMER.
ECOO157:CRP-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ACK0.

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

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.
  2. "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12."
    Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.
    , Kuhara S., Shiba T., Hattori M., Shinagawa H.
    DNA Res. 8:11-22(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Entry informationi

Entry nameiCRP_ECO57
AccessioniPrimary (citable) accession number: P0ACK0
Secondary accession number(s): P03020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 1, 2014
This is version 72 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

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3