CRPL_MYCTO
ID CRPL_MYCTO Reviewed; 224 AA.
AC P9WMH2; F2GFB8; L0TDH2; O69644; Q7D534;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 42.
DE RecName: Full=CRP-like cAMP-activated global transcriptional regulator {ECO:0000250|UniProtKB:P9WMH3};
DE AltName: Full=cAMP receptor protein {ECO:0000303|PubMed:16946269};
DE Short=CRP {ECO:0000303|PubMed:16946269};
DE AltName: Full=cAMP regulatory protein {ECO:0000303|PubMed:16946269};
GN Name=crp {ECO:0000250|UniProtKB:P9WMH3}; OrderedLocusNames=MT3777;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
RN [2]
RP FUNCTION, AND DNA-BINDING.
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=16946269; DOI=10.1099/mic.0.28924-0;
RA Agarwal N., Raghunand T.R., Bishai W.R.;
RT "Regulation of the expression of whiB1 in Mycobacterium tuberculosis: role
RT of cAMP receptor protein.";
RL Microbiology 152:2749-2756(2006).
CC -!- FUNCTION: Global transcriptional regulator that complexes with cAMP and
CC binds to specific DNA promoter sites, causing DNA-bending, to regulate
CC transcription. cAMP improves binding to specific DNA sequences,
CC probably by altering protein conformation. Activates expression of
CC whiB1. {ECO:0000269|PubMed:16946269}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P9WMH3}.
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DR EMBL; AE000516; AAK48144.1; -; Genomic_DNA.
DR PIR; E70790; E70790.
DR RefSeq; WP_003419728.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMH2; -.
DR SMR; P9WMH2; -.
DR PRIDE; P9WMH2; -.
DR EnsemblBacteria; AAK48144; AAK48144; MT3777.
DR KEGG; mtc:MT3777; -.
DR PATRIC; fig|83331.31.peg.4067; -.
DR HOGENOM; CLU_075053_3_4_11; -.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0030552; F:cAMP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; 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; IPR000595; cNMP-bd_dom.
DR InterPro; IPR012318; HTH_CRP.
DR InterPro; IPR014710; RmlC-like_jellyroll.
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 SMART; SM00100; cNMP; 1.
DR SMART; SM00419; HTH_CRP; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR PROSITE; PS50042; CNMP_BINDING_3; 1.
DR PROSITE; PS51063; HTH_CRP_2; 1.
PE 1: Evidence at protein level;
KW Activator; cAMP; cAMP-binding; DNA-binding; Nucleotide-binding; Repressor;
KW Transcription; Transcription regulation; Virulence.
FT CHAIN 1..224
FT /note="CRP-like cAMP-activated global transcriptional
FT regulator"
FT /id="PRO_0000427304"
FT DOMAIN 144..217
FT /note="HTH crp-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT DNA_BIND 177..196
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00387"
FT BINDING 64..70
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
FT BINDING 79..82
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WMH3"
FT BINDING 89..90
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WMH3"
FT BINDING 134..135
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P9WMH3"
FT BINDING 142..143
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
FT BINDING 178..188
FT /ligand="3',5'-cyclic AMP"
FT /ligand_id="ChEBI:CHEBI:58165"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0ACJ8"
SQ SEQUENCE 224 AA; 24791 MW; BAB89A61B64839E3 CRC64;
MDEILARAGI FQGVEPSAIA ALTKQLQPVD FPRGHTVFAE GEPGDRLYII ISGKVKIGRR
APDGRENLLT IMGPSDMFGE LSIFDPGPRT SSATTITEVR AVSMDRDALR SWIADRPEIS
EQLLRVLARR LRRTNNNLAD LIFTDVPGRV AKQLLQLAQR FGTQEGGALR VTHDLTQEEI
AQLVGASRET VNKALADFAH RGWIRLEGKS VLISDSERLA RRAR
