ID   KMTR_MYCTU              Reviewed;         130 AA.
AC   O53838; F2GNU2; L0T4V7;
DT   03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 3.
DT   25-MAY-2022, entry version 131.
DE   RecName: Full=HTH-type transcriptional regulator KmtR;
GN   Name=kmtR; OrderedLocusNames=Rv0827c;
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   FUNCTION, DNA-BINDING, ACTIVITY REGULATION, INDUCTION, GENE NAME, AND
RP   MUTAGENESIS OF CYS-16; HIS-88; GLU-101; HIS-102; HIS-110 AND HIS-111.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=17726022; DOI=10.1074/jbc.m703451200;
RA   Campbell D.R., Chapman K.E., Waldron K.J., Tottey S., Kendall S.,
RA   Cavallaro G., Andreini C., Hinds J., Stoker N.G., Robinson N.J.,
RA   Cavet J.S.;
RT   "Mycobacterial cells have dual nickel-cobalt sensors: sequence
RT   relationships and metal sites of metal-responsive repressors are not
RT   congruent.";
RL   J. Biol. Chem. 282:32298-32310(2007).
CC   -!- FUNCTION: Represses expression of Rv2025c and its own expression. Acts
CC       by binding to the promoter regions. {ECO:0000269|PubMed:17726022}.
CC   -!- ACTIVITY REGULATION: Binding to DNA is inhibited by nickel and cobalt
CC       ions. {ECO:0000269|PubMed:17726022}.
CC   -!- INDUCTION: Negatively autoregulated. {ECO:0000269|PubMed:17726022}.
CC   -!- MISCELLANEOUS: KmtR has tighter affinities for nickel and cobalt than
CC       NmtR. {ECO:0000305|PubMed:17726022}.
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DR   EMBL; AL123456; CCP43575.1; -; Genomic_DNA.
DR   PIR; C70811; C70811.
DR   RefSeq; NP_215342.1; NC_000962.3.
DR   RefSeq; WP_003404335.1; NZ_NVQJ01000066.1.
DR   AlphaFoldDB; O53838; -.
DR   SMR; O53838; -.
DR   STRING; 83332.Rv0827c; -.
DR   PaxDb; O53838; -.
DR   DNASU; 885375; -.
DR   GeneID; 885375; -.
DR   KEGG; mtu:Rv0827c; -.
DR   PATRIC; fig|83332.111.peg.914; -.
DR   TubercuList; Rv0827c; -.
DR   eggNOG; COG0640; Bacteria.
DR   InParanoid; O53838; -.
DR   OMA; HTRREGT; -.
DR   PhylomeDB; O53838; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IDA:MTBBASE.
DR   GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR   GO; GO:0032025; P:response to cobalt ion; IDA:MTBBASE.
DR   GO; GO:0010045; P:response to nickel cation; IDA: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; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..130
FT                   /note="HTH-type transcriptional regulator KmtR"
FT                   /id="PRO_0000419178"
FT   DOMAIN          10..104
FT                   /note="HTH arsR-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   DNA_BIND        44..67
FT                   /note="H-T-H motif"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT   REGION          110..130
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         16
FT                   /note="C->S: No change in activity. Does not affect
FT                   regulation by metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
FT   MUTAGEN         88
FT                   /note="H->Q: No change in activity. Lack of regulation by
FT                   metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
FT   MUTAGEN         101
FT                   /note="E->Q: No change in activity. Lack of regulation by
FT                   metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
FT   MUTAGEN         102
FT                   /note="H->Q: No change in activity. Lack of regulation by
FT                   metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
FT   MUTAGEN         110
FT                   /note="H->Q: No change in activity. Lack of regulation by
FT                   metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
FT   MUTAGEN         111
FT                   /note="H->Q: No change in activity. Lack of regulation by
FT                   metal ions."
FT                   /evidence="ECO:0000269|PubMed:17726022"
SQ   SEQUENCE   130 AA;  14296 MW;  DC6C2FD5B599D1A2 CRC64;
     MYADSGPDPL PDDQVCLVVE VFRMLADATR VQVLWSLADR EMSVNELAEQ VGKPAPSVSQ
     HLAKLRMARL VRTRRDGTTI FYRLENEHVR QLVIDAVFNA EHAGPGIPRH HRAAGGLQSV
     AKASATKDVG