CRP_SHIFL
ID CRP_SHIFL Reviewed; 210 AA.
AC P0ACK1; P03020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SF3376, S4387;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 12022 / CDC 3591-52 / Serotype 2b;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; M13772; AAA26515.1; -; Genomic_DNA.
DR EMBL; AE005674; AAN44839.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP19339.1; -; Genomic_DNA.
DR RefSeq; NP_709132.1; NC_004337.2.
DR RefSeq; WP_000242755.1; NZ_WPGW01000003.1.
DR AlphaFoldDB; P0ACK1; -.
DR SMR; P0ACK1; -.
DR STRING; 198214.SF3376; -.
DR EnsemblBacteria; AAN44839; AAN44839; SF3376.
DR EnsemblBacteria; AAP19339; AAP19339; S4387.
DR GeneID; 1026956; -.
DR GeneID; 67450219; -.
DR KEGG; sfl:SF3376; -.
DR KEGG; sfx:S4387; -.
DR PATRIC; fig|198214.7.peg.3986; -.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; VLCRDFG; -.
DR OrthoDB; 1596937at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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..210
FT /note="cAMP-activated global transcriptional regulator CRP"
FT /id="PRO_0000100151"
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"
SQ SEQUENCE 210 AA; 23640 MW; DCBC24FA46C61B3D CRC64;
MVLGKPQTDP TLEWFLSHCH IHKYPSKSTL IHQGEKAETL YYIVKGSVAV LIKDEEGKEM
ILSYLNQGDF IGELGLFEEG QERSAWVRAK TACEVAEISY KKFRQLIQVN PDILMRLSAQ
MARRLQVTSE KVGNLAFLDV TGRIAQTLLN LAKQPDAMTH PDGMQIKITR QEIGQIVGCS
RETVGRILKM LEDQNLISAH GKTIVVYGTR
