ID CRP_SALTY Reviewed; 210 AA. AC P0A2T6; P06170; P29282; DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1988, sequence version 1. DT 27-MAR-2024, entry version 111. 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; Synonyms=cap; OrderedLocusNames=STM3466; OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=99287; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=3525518; DOI=10.1128/jb.167.2.639-646.1986; RA Cossart P., Groisman E.A., Serre M.-C., Casadaban M.J., Gicquel-Sanzey B.; RT "crp genes of Shigella flexneri, Salmonella typhimurium, and Escherichia RT coli."; RL J. Bacteriol. 167:639-646(1986). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF LYS-131. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=3015882; DOI=10.1128/jb.167.2.616-622.1986; RA Schroeder C.J., Dobrogosz W.J.; RT "Cloning and DNA sequence analysis of the wild-type and mutant cyclic AMP RT receptor protein genes from Salmonella typhimurium."; RL J. Bacteriol. 167:616-622(1986). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LT2 / SGSC1412 / ATCC 700720; RX PubMed=11677609; DOI=10.1038/35101614; RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E., RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., RA Wilson R.K.; RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."; RL Nature 413:852-856(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; M13773; AAA27039.1; -; Genomic_DNA. DR EMBL; M13770; AAA62414.1; -; Genomic_DNA. DR EMBL; AE006468; AAL22328.1; -; Genomic_DNA. DR PIR; A26049; A26049. DR RefSeq; NP_462369.1; NC_003197.2. DR RefSeq; WP_000242758.1; NC_003197.2. DR AlphaFoldDB; P0A2T6; -. DR BMRB; P0A2T6; -. DR SMR; P0A2T6; -. DR STRING; 99287.STM3466; -. DR PaxDb; 99287-STM3466; -. DR GeneID; 1254989; -. DR GeneID; 85160134; -. DR KEGG; stm:STM3466; -. DR PATRIC; fig|99287.12.peg.3663; -. DR HOGENOM; CLU_075053_3_5_6; -. DR OMA; AFTRVEM; -. DR PhylomeDB; P0A2T6; -. DR BioCyc; SENT99287:STM3466-MONOMER; -. DR PHI-base; PHI:2684; -. DR PRO; PR:P0A2T6; -. DR Proteomes; UP000001014; Chromosome. DR CollecTF; EXPREG_00000730; -. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0032993; C:protein-DNA complex; IMP:CollecTF. DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW. DR GO; GO:0001216; F:DNA-binding transcription activator activity; IMP:CollecTF. DR GO; GO:0003700; F:DNA-binding transcription factor activity; IBA:GO_Central. DR GO; GO:0000976; F:transcription cis-regulatory region binding; IMP:CollecTF. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IEP:CollecTF. 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 1: Evidence at protein level; KW Acetylation; Activator; cAMP; cAMP-binding; DNA-binding; KW Nucleotide-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1..210 FT /note="cAMP-activated global transcriptional regulator CRP" FT /id="PRO_0000100150" FT DOMAIN 138..210 FT /note="HTH crp-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT DNA_BIND 180..186 FT /note="H-T-H motif" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387" FT REGION 20..22 FT /note="Activating region 2 (AR2); probably contacts the N- FT terminus of RpoA" FT /evidence="ECO:0000250" FT REGION 53..59 FT /note="Activating region 3 (AR3); probably contacts sigma- FT 70 (RpoD)" FT /evidence="ECO:0000250" FT REGION 154..163 FT /note="Activating region 1 (AR1); probably contacts the C- FT terminus of RpoA" FT /evidence="ECO:0000250" FT BINDING 57..63 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 72..74 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 83..84 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 128..129 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="1" FT /evidence="ECO:0000250" FT BINDING 136..137 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT /evidence="ECO:0000250" FT BINDING 171..181 FT /ligand="3',5'-cyclic AMP" FT /ligand_id="ChEBI:CHEBI:58165" FT /ligand_label="2" FT /evidence="ECO:0000250" FT SITE 97 FT /note="Activating region 2 (AR2); probably contacts the N- FT terminus of RpoA" FT /evidence="ECO:0000250" FT SITE 102 FT /note="Activating region 2 (AR2); probably contacts the N- FT terminus of RpoA" FT /evidence="ECO:0000250" FT MOD_RES 101 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250" FT MUTAGEN 131 FT /note="K->Q,T: In acr-4 and acr-3 respectively; higher FT levels of cAMP synthesis." FT /evidence="ECO:0000269|PubMed:3015882" FT CONFLICT 40 FT /note="L -> S (in Ref. 2; AAA62414)" FT /evidence="ECO:0000305" FT CONFLICT 119 FT /note="S -> A (in Ref. 2; AAA62414)" FT /evidence="ECO:0000305" SQ SEQUENCE 210 AA; 23656 MW; C54244E974D53A0F CRC64; MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY KKFRQLIQVN PDILMRLSSQ MARRLQVTSE KVGNLAFLDV TGRIAQTLLN LAKQPDAMTH PDGMQIKITR QEIGQIVGCS RETVGRILKM LEDQNLISAH GKTIVVYGTR //