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SMTB_MYCTU
ID   SMTB_MYCTU              Reviewed;         135 AA.
AC   P9WMI5; F2GIN4; L0TCA4; O05840; Q7D7A0;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 41.
DE   RecName: Full=HTH-type transcriptional repressor SmtB;
GN   Name=smtB; OrderedLocusNames=Rv2358;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   INDUCTION.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15059632; DOI=10.1016/j.resmic.2003.11.009;
RA   Milano A., Branzoni M., Canneva F., Profumo A., Riccardi G.;
RT   "The Mycobacterium tuberculosis Rv2358-furB operon is induced by zinc.";
RL   Res. Microbiol. 155:192-200(2004).
RN   [3]
RP   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, AND INDUCTION.
RX   PubMed=16077132; DOI=10.1128/jb.187.16.5837-5840.2005;
RA   Canneva F., Branzoni M., Riccardi G., Provvedi R., Milano A.;
RT   "Rv2358 and FurB: two transcriptional regulators from Mycobacterium
RT   tuberculosis which respond to zinc.";
RL   J. Bacteriol. 187:5837-5840(2005).
RN   [4]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA   Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA   Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA   Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA   Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT   mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Transcriptional regulator involved in zinc homeostasis.
CC       Represses the expression of the smtB-zur operon in the absence of zinc.
CC       Could act as the metal sensor that controls the expression of zur in
CC       response to zinc availability. {ECO:0000269|PubMed:16077132}.
CC   -!- ACTIVITY REGULATION: Binding to DNA is inhibited by zinc ions.
CC       {ECO:0000269|PubMed:16077132}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INDUCTION: Induced by zinc. Negatively autoregulated.
CC       {ECO:0000269|PubMed:15059632, ECO:0000269|PubMed:16077132}.
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DR   EMBL; AL123456; CCP45146.1; -; Genomic_DNA.
DR   PIR; E70585; E70585.
DR   RefSeq; NP_216874.1; NC_000962.3.
DR   RefSeq; WP_003412205.1; NZ_NVQJ01000029.1.
DR   AlphaFoldDB; P9WMI5; -.
DR   SMR; P9WMI5; -.
DR   STRING; 83332.Rv2358; -.
DR   PaxDb; P9WMI5; -.
DR   DNASU; 888965; -.
DR   GeneID; 45426345; -.
DR   GeneID; 888965; -.
DR   KEGG; mtu:Rv2358; -.
DR   TubercuList; Rv2358; -.
DR   eggNOG; COG0640; Bacteria.
DR   OMA; GREVMYR; -.
DR   PhylomeDB; P9WMI5; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0010043; P:response to zinc ion; IGI:MTBBASE.
DR   CDD; cd00090; HTH_ARSR; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR011991; ArsR-like_HTH.
DR   InterPro; IPR001845; HTH_ArsR_DNA-bd_dom.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   Pfam; PF01022; HTH_5; 1.
DR   PRINTS; PR00778; HTHARSR.
DR   SMART; SM00418; HTH_ARSR; 1.
DR   SUPFAM; SSF46785; SSF46785; 1.
DR   PROSITE; PS50987; HTH_ARSR_2; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Metal-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation; Zinc.
FT   CHAIN           1..135
FT                   /note="HTH-type transcriptional repressor SmtB"
FT                   /id="PRO_0000419166"
FT   DOMAIN          40..134
FT                   /note="HTH arsR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   DNA_BIND        74..97
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         129
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   BINDING         132
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
SQ   SEQUENCE   135 AA;  14421 MW;  B64B284BB9AD5D6B CRC64;
     MVTSPSTPTA AHEDVGADEV GGHQHPADRF AECPTFPAPP PREILDAAGE LLRALAAPVR
     IAIVLQLRES QRCVHELVDA LHVPQPLVSQ HLKILKAAGV VTGERSGREV LYRLADHHLA
     HIVLDAVAHA GEDAI
 
 
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