CRP_PASMU
ID CRP_PASMU Reviewed; 209 AA.
AC O05689;
DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=cAMP-activated global transcriptional regulator CRP;
DE AltName: Full=Catabolite activator protein;
DE Short=CAP;
DE AltName: Full=Catabolite gene activator;
DE AltName: Full=cAMP receptor protein;
DE Short=CRP;
DE AltName: Full=cAMP regulatory protein;
GN Name=crp; OrderedLocusNames=PM1157;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Roland K.L., Mukkur T.K., Ball T.K.;
RT "Isolation and characterization of crp mutants in Pasteurella multocida.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- FUNCTION: A global transcription regulator. Complexes with cyclic AMP
CC (cAMP) which allosterically activates DNA binding to regulate
CC transcription. It can act as an activator, repressor, coactivator or
CC corepressor. Induces a severe bend in DNA. Acts as a negative regulator
CC of its own synthesis as well as for adenylate cyclase (cyaA), which
CC generates cAMP. Plays a major role in carbon catabolite repression
CC (CCR) (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer, which upon binding cAMP is able to bind DNA. Binds
CC the N- and C-terminus of RNA polymerase subunit RpoA and sigma-70
CC (RpoD) (By similarity). {ECO:0000250}.
CC -!- DOMAIN: The N-terminal domain binds cAMP and is responsible for
CC homodimerization, while the C-terminal domain binds DNA when cAMP is
CC bound. {ECO:0000250}.
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DR EMBL; U95380; AAB53064.1; -; Genomic_DNA.
DR EMBL; AE004439; AAK03241.1; -; Genomic_DNA.
DR RefSeq; WP_010907050.1; NC_002663.1.
DR AlphaFoldDB; O05689; -.
DR SMR; O05689; -.
DR STRING; 747.DR93_811; -.
DR EnsemblBacteria; AAK03241; AAK03241; PM1157.
DR GeneID; 62225086; -.
DR KEGG; pmu:PM1157; -.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; VLCRDFG; -.
DR Proteomes; UP000000809; Chromosome.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR CDD; cd00038; CAP_ED; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR Gene3D; 2.60.120.10; -; 1.
DR InterPro; IPR018490; cNMP-bd-like.
DR InterPro; IPR018488; cNMP-bd_CS.
DR InterPro; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR InterPro; IPR018335; Tscrpt_reg_HTH_Crp-type_CS.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00027; cNMP_binding; 1.
DR Pfam; PF13545; HTH_Crp_2; 1.
DR PRINTS; PR00034; HTHCRP.
DR SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS00888; CNMP_BINDING_1; 1.
DR PROSITE; PS00889; CNMP_BINDING_2; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS00042; HTH_CRP_1; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 3: Inferred from homology;
KW Acetylation; Activator; cAMP; cAMP-binding; DNA-binding;
KW Nucleotide-binding; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..209
FT /note="cAMP-activated global transcriptional regulator CRP"
FT /id="PRO_0000100149"
FT DOMAIN 137..209
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 179..185
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT REGION 19..21
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT REGION 52..58
FT /note="Activating region 3 (AR3); probably contacts sigma-
FT 70 (RpoD)"
FT /evidence="ECO:0000250"
FT REGION 153..162
FT /note="Activating region 1 (AR1); probably contacts the C-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT BINDING 56..62
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 71..73
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 82..83
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 127..128
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 135..136
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 170..180
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT SITE 96
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT SITE 101
FT /note="Activating region 2 (AR2); probably contacts the N-
FT terminus of RpoA"
FT /evidence="ECO:0000250"
FT MOD_RES 100
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 209 AA; 23541 MW; 2E6A60E75F9CEF07 CRC64;
MQTTPSIDPT LEWFLSHCHI HKYPSKSTLI HAGEKAETLY YLIKGSVAVL VKDEDGKEMI
LTYLSQGDFF GEAGLFEEGQ LRSAWIKAKS PCEIAEISYK KFRQLIQVNP DILMHLSAQL
ARRLQNTSRQ VSNLAFLDVT GRIAQTLLNL AKMPEAMTHP DGMQIKITRQ EIGQMVGCSR
ETVGRILKML EDQHLISAHG KTIVVYGTR
