NMTR_MYCTU
ID NMTR_MYCTU Reviewed; 120 AA.
AC O69711; L0TGE5;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 3.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=HTH-type transcriptional regulator NmtR;
GN Name=nmtR; OrderedLocusNames=Rv3744;
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, GENE NAME, AND MUTAGENESIS OF
RP ASP-51; ASP-91; HIS-93; HIS-104; HIS-107; HIS-109; ASP-114 AND HIS-116.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=12163508; DOI=10.1074/jbc.m207677200;
RA Cavet J.S., Meng W., Pennella M.A., Appelhoff R.J., Giedroc D.P.,
RA Robinson N.J.;
RT "A nickel-cobalt-sensing ArsR-SmtB family repressor. Contributions of
RT cytosol and effector binding sites to metal selectivity.";
RL J. Biol. Chem. 277:38441-38448(2002).
RN [3]
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).
RN [4]
RP STRUCTURE BY NMR, ACTIVITY REGULATION, SUBUNIT, MASS SPECTROMETRY, AND
RP NICKEL-BINDING SITES.
RX PubMed=22394357; DOI=10.1021/bi3001402;
RA Lee C.W., Chakravorty D.K., Chang F.M., Reyes-Caballero H., Ye Y.,
RA Merz K.M. Jr., Giedroc D.P.;
RT "Solution structure of Mycobacterium tuberculosis NmtR in the apo state:
RT insights into Ni(II)-mediated allostery.";
RL Biochemistry 51:2619-2629(2012).
CC -!- FUNCTION: Represses transcription of ctpJ/nmtA, by binding to its
CC promoter region. {ECO:0000269|PubMed:12163508}.
CC -!- ACTIVITY REGULATION: Binding to DNA is inhibited by nickel and, to some
CC extent, cobalt ions. {ECO:0000269|PubMed:12163508,
CC ECO:0000269|PubMed:22394357}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22394357}.
CC -!- MASS SPECTROMETRY: Mass=12699.7; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:22394357};
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DR EMBL; AL123456; CCP46571.1; -; Genomic_DNA.
DR PIR; A70799; A70799.
DR RefSeq; NP_218261.1; NC_000962.3.
DR RefSeq; WP_003901716.1; NZ_NVQJ01000009.1.
DR AlphaFoldDB; O69711; -.
DR BMRB; O69711; -.
DR SMR; O69711; -.
DR STRING; 83332.Rv3744; -.
DR PaxDb; O69711; -.
DR DNASU; 885418; -.
DR GeneID; 45427743; -.
DR GeneID; 885418; -.
DR KEGG; mtu:Rv3744; -.
DR TubercuList; Rv3744; -.
DR eggNOG; COG0640; Bacteria.
DR InParanoid; O69711; -.
DR OMA; YHVEHLR; -.
DR PhylomeDB; O69711; -.
DR PRO; PR:O69711; -.
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 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; Nickel; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..120
FT /note="HTH-type transcriptional regulator NmtR"
FT /id="PRO_0000419179"
FT DOMAIN 15..109
FT /note="HTH arsR-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT DNA_BIND 49..72
FT /note="H-T-H motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00340"
FT BINDING 91
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT BINDING 93
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT BINDING 104
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT BINDING 107
FT /ligand="Ni(2+)"
FT /ligand_id="ChEBI:CHEBI:49786"
FT MUTAGEN 51
FT /note="D->A: Does not affect activity and regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 91
FT /note="D->A: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 93
FT /note="H->R: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 104
FT /note="H->R: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 107
FT /note="H->R: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 109
FT /note="H->R: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 114
FT /note="D->A: Does not affect activity and regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
FT MUTAGEN 116
FT /note="H->R: No change in activity. Lack of regulation by
FT metal ions."
FT /evidence="ECO:0000269|PubMed:12163508"
SQ SEQUENCE 120 AA; 12836 MW; EC9D7491B06A61E5 CRC64;
MGHGVEGRNR PSAPLDSQAA AQVASTLQAL ATPSRLMILT QLRNGPLPVT DLAEAIGMEQ
SAVSHQLRVL RNLGLVVGDR AGRSIVYSLY DTHVAQLLDE AIYHSEHLHL GLSDRHPSAG
