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 27-MAR-2024, entry version 146. 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; Pseudomonadota; 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 272843.PM1157; -. DR EnsemblBacteria; AAK03241; AAK03241; PM1157. DR GeneID; 77206473; -. DR KEGG; pmu:PM1157; -. DR HOGENOM; CLU_075053_3_5_6; -. DR OrthoDB; 61906at2; -. 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 CDD; cd00092; HTH_CRP; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1. DR InterPro; IPR018488; cNMP-bd_CS. DR InterPro; IPR000595; cNMP-bd_dom. DR InterPro; IPR018490; cNMP-bd_dom_sf. 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 PANTHER; PTHR24567:SF79; CAMP-ACTIVATED GLOBAL TRANSCRIPTIONAL REGULATOR CRP; 1. DR PANTHER; PTHR24567; CRP FAMILY TRANSCRIPTIONAL REGULATORY PROTEIN; 1. 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; SSF51206; cAMP-binding domain-like; 1. DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 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 //