CRP_SALTY
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 03-AUG-2022, entry version 102.
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; Proteobacteria; 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}.
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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; P0A2T6; -.
DR EnsemblBacteria; AAL22328; AAL22328; STM3466.
DR GeneID; 1254989; -.
DR GeneID; 7962173; -.
DR KEGG; stm:STM3466; -.
DR PATRIC; fig|99287.12.peg.3663; -.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; VLCRDFG; -.
DR PhylomeDB; P0A2T6; -.
DR BioCyc; SENT99287:STM3466-MON; -.
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 transcription, DNA-templated; IEP:CollecTF.
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 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
