SMTB_MYCTO
ID SMTB_MYCTO Reviewed; 135 AA.
AC P9WMI4; 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 42.
DE RecName: Full=HTH-type transcriptional repressor SmtB;
GN Name=smtB; OrderedLocusNames=MT2427;
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).
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 (By similarity). {ECO:0000250}.
CC -!- ACTIVITY REGULATION: Binding to DNA is inhibited by zinc ions.
CC {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {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; AE000516; AAK46721.1; -; Genomic_DNA.
DR PIR; E70585; E70585.
DR RefSeq; WP_003412205.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WMI4; -.
DR SMR; P9WMI4; -.
DR EnsemblBacteria; AAK46721; AAK46721; MT2427.
DR GeneID; 45426345; -.
DR KEGG; mtc:MT2427; -.
DR PATRIC; fig|83331.31.peg.2615; -.
DR HOGENOM; CLU_097806_7_6_11; -.
DR Proteomes; UP000001020; 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 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 3: Inferred from homology;
KW DNA-binding; Metal-binding; Repressor; Transcription;
KW Transcription regulation; Zinc.
FT CHAIN 1..135
FT /note="HTH-type transcriptional repressor SmtB"
FT /id="PRO_0000427298"
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