ID   HTM_MYCBP               Reviewed;         241 AA.
AC   A1KG37;
DT   31-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 68.
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=BCG_0605c;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BCG / Pasteur 1173P2;
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W., Valenti P.,
RA   Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C., Inwald J.K.,
RA   Golby P., Garcia J.N., Hewinson R.G., Behr M.A., Quail M.A., Churcher C.,
RA   Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND INDUCTION.
RC   STRAIN=BCG / Pasteur 1173P2;
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:0000250|UniProtKB:A5TZU0}.
CC   -!- INDUCTION: By salicylate (at protein level).
CC       {ECO:0000269|PubMed:11583850}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; AM408590; CAL70590.1; -; Genomic_DNA.
DR   RefSeq; WP_003402938.1; NC_008769.1.
DR   AlphaFoldDB; A1KG37; -.
DR   SMR; A1KG37; -.
DR   KEGG; mbb:BCG_0605c; -.
DR   HOGENOM; CLU_056435_4_2_11; -.
DR   OMA; EIRPARI; -.
DR   Proteomes; UP000001472; 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_0000419775"
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