ID   HTM_MYCTA               Reviewed;         241 AA.
AC   A5TZU0;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=MRA_0567;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
RN   [2]
RP   SUBCELLULAR LOCATION, AND INDUCTION.
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=11583850; DOI=10.1111/j.1574-6968.2001.tb10843.x;
RA   Sun Z., Cheng S.J., Zhang H., Zhang Y.;
RT   "Salicylate uniquely induces a 27-kDa protein in tubercle bacillus.";
RL   FEMS Microbiol. Lett. 203:211-216(2001).
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:0000269|PubMed:11583850}.
CC   -!- INDUCTION: By salicylate and at higher concentrations by para-
CC       aminosalicylate (PAS) (at protein level).
CC       {ECO:0000269|PubMed:11583850}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP000611; ABQ72290.1; -; Genomic_DNA.
DR   RefSeq; WP_003402938.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5TZU0; -.
DR   SMR; A5TZU0; -.
DR   STRING; 419947.MRA_0567; -.
DR   EnsemblBacteria; ABQ72290; ABQ72290; MRA_0567.
DR   KEGG; mra:MRA_0567; -.
DR   eggNOG; COG2226; Bacteria.
DR   HOGENOM; CLU_056435_4_2_11; -.
DR   OMA; EIRPARI; -.
DR   OrthoDB; 2049098at2; -.
DR   Proteomes; UP000001988; 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   1: Evidence at protein level;
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_0000419776"
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