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O05689

- CRP_PASMU

UniProt

O05689 - CRP_PASMU

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
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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

    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

    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

    MQTTPSIDPT LEWFLSHCHI HKYPSKSTLI HAGEKAETLY YLIKGSVAVL    50
    VKDEDGKEMI LTYLSQGDFF GEAGLFEEGQ LRSAWIKAKS PCEIAEISYK 100
    KFRQLIQVNP DILMHLSAQL ARRLQNTSRQ VSNLAFLDVT GRIAQTLLNL 150
    AKMPEAMTHP DGMQIKITRQ EIGQMVGCSR ETVGRILKML EDQHLISAHG 200
    KTIVVYGTR 209
    Length:209
    Mass (Da):23,541
    Last modified:July 1, 1997 - v1
    Checksum:i2E6A60E75F9CEF07
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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

    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