ID   HTM_MYCTO               Reviewed;         241 AA.
AC   P9WKL4; F2GMK5; L0T6V5; O06426; Q7D9M8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 35.
DE   RecName: Full=2-heptyl-1-hydroxyquinolin-4(1H)-one methyltransferase {ECO:0000250|UniProtKB:P9WKL5};
DE            Short=HQNO methyltransferase {ECO:0000250|UniProtKB:P9WKL5};
DE            Short=HQNO-MTase {ECO:0000250|UniProtKB:P9WKL5};
DE            EC=2.1.1.374 {ECO:0000250|UniProtKB:P9WKL5};
DE   AltName: Full=Heterocyclic toxin methyltransferase {ECO:0000250|UniProtKB:P9WKL5};
GN   Name=htm {ECO:0000250|UniProtKB:P9WKL5}; OrderedLocusNames=MT0586;
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: Involved in cellular response to chemical stress and may
CC       contribute to resistance toward antimicrobial natural compounds as well
CC       as drugs. Catalyzes the methylation and detoxification of the
CC       P.aeruginosa toxin 2-heptyl-1-hydroxy-4(1H)-quinolinone (HQNO) to 2-
CC       heptyl-1-methoxy-4(1H)-quinolinone (HMOQ).
CC       {ECO:0000250|UniProtKB:P9WKL5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-heptyl-1-hydroxy-4(1H)-quinolinone + S-adenosyl-L-methionine
CC         = 2-heptyl-1-methoxy-4(1H)-quinolinone + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:65924, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:157768,
CC         ChEBI:CHEBI:157769; EC=2.1.1.374;
CC         Evidence={ECO:0000250|UniProtKB:P9WKL5};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65925;
CC         Evidence={ECO:0000250|UniProtKB:P9WKL5};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P9WKL5}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A5TZU0}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
CC       {ECO:0000305}.
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DR   EMBL; AE000516; AAK44809.1; -; Genomic_DNA.
DR   PIR; C70549; C70549.
DR   RefSeq; WP_003402938.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WKL4; -.
DR   SMR; P9WKL4; -.
DR   EnsemblBacteria; AAK44809; AAK44809; MT0586.
DR   KEGG; mtc:MT0586; -.
DR   PATRIC; fig|83331.31.peg.617; -.
DR   HOGENOM; CLU_056435_4_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR041698; Methyltransf_25.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF13649; Methyltransf_25; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..241
FT                   /note="2-heptyl-1-hydroxyquinolin-4(1H)-one
FT                   methyltransferase"
FT                   /id="PRO_0000427633"
SQ   SEQUENCE   241 AA;  25945 MW;  32652F8B609D5170 CRC64;
     MSTVLTYIRA VDIYEHMTES LDLEFESAYR GESVAFGEGV RPPWSIGEPQ PELAALIVQG
     KFRGDVLDVG CGEAAISLAL AERGHTTVGL DLSPAAVELA RHEAAKRGLA NASFEVADAS
     SFTGYDGRFD TIVDSTLFHS MPVESREGYL QSIVRAAAPG ASYFVLVFDR AAIPEGPINA
     VTEDELRAAV SKYWIIDEIK PARLYARFPA GFAGMPALLD IREEPNGLQS IGGWLLSAHL
     G