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Protein

cAMP-activated global transcriptional regulator CRP

Gene

crp

Organism
Shigella flexneri
Status
Reviewed-Annotation score: 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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

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

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:SF3376, S4387
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 210210cAMP-activated global transcriptional regulator CRPPRO_0000100151Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ACK1.
PRIDEiP0ACK1.

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

STRINGi198214.SF3376.

Structurei

3D structure databases

ProteinModelPortaliP0ACK1.
SMRiP0ACK1. Positions 9-208.
ModBaseiSearch...
MobiDBiSearch...

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.
OMAiKTMVVYG.
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.

P0ACK1-1 [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
M13772 Genomic DNA. Translation: AAA26515.1.
AE005674 Genomic DNA. Translation: AAN44839.1.
AE014073 Genomic DNA. Translation: AAP19339.1.
RefSeqiNP_709132.1. NC_004337.2.
WP_000242755.1. NZ_LM651928.1.

Genome annotation databases

EnsemblBacteriaiAAN44839; AAN44839; SF3376.
AAP19339; AAP19339; S4387.
GeneIDi1026956.
KEGGisfl:SF3376.
PATRICi18710780. VBIShiFle31049_4794.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M13772 Genomic DNA. Translation: AAA26515.1.
AE005674 Genomic DNA. Translation: AAN44839.1.
AE014073 Genomic DNA. Translation: AAP19339.1.
RefSeqiNP_709132.1. NC_004337.2.
WP_000242755.1. NZ_LM651928.1.

3D structure databases

ProteinModelPortaliP0ACK1.
SMRiP0ACK1. Positions 9-208.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF3376.

Proteomic databases

PaxDbiP0ACK1.
PRIDEiP0ACK1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN44839; AAN44839; SF3376.
AAP19339; AAP19339; S4387.
GeneIDi1026956.
KEGGisfl:SF3376.
PATRICi18710780. VBIShiFle31049_4794.

Phylogenomic databases

eggNOGiCOG0664.
HOGENOMiHOG000250565.
KOiK10914.
OMAiKTMVVYG.
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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: ATCC 12022 / CDC 3591-52 / Serotype 2b.
  2. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiCRP_SHIFL
AccessioniPrimary (citable) accession number: P0ACK1
Secondary accession number(s): P03020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 22, 2015
This is version 75 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.