CRP_ECO57
ID CRP_ECO57 Reviewed; 210 AA.
AC P0ACK0; P03020;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=Z4718, ECs4208;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(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; AE005174; AAG58465.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB37631.1; -; Genomic_DNA.
DR PIR; E86000; E86000.
DR PIR; H91154; H91154.
DR RefSeq; NP_312235.1; NC_002695.1.
DR RefSeq; WP_000242755.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0ACK0; -.
DR BMRB; P0ACK0; -.
DR SMR; P0ACK0; -.
DR STRING; 155864.EDL933_4561; -.
DR PRIDE; P0ACK0; -.
DR EnsemblBacteria; AAG58465; AAG58465; Z4718.
DR EnsemblBacteria; BAB37631; BAB37631; ECs_4208.
DR GeneID; 67450219; -.
DR GeneID; 915936; -.
DR KEGG; ece:Z4718; -.
DR KEGG; ecs:ECs_4208; -.
DR PATRIC; fig|386585.9.peg.4392; -.
DR eggNOG; COG0664; Bacteria.
DR HOGENOM; CLU_075053_3_5_6; -.
DR OMA; VLCRDFG; -.
DR EvolutionaryTrace; P0ACK0; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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_0000100145"
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
