ID   MTF2_MYCS2              Reviewed;         274 AA.
AC   Q9RMN9; A0QPG8; Q2YHH6;
DT   03-SEP-2014, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Fatty-acid O-methyltransferase;
DE            Short=fmt;
DE            EC=2.1.1.15;
GN   Name=mtf2; OrderedLocusNames=MSMEI_0386, MSMEG_0393;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=12368441; DOI=10.1099/00221287-148-10-3079;
RA   Jeevarajah D., Patterson J.H., McConville M.J., Billman-Jacobe H.;
RT   "Modification of glycopeptidolipids by an O-methyltransferase of
RT   Mycobacterium smegmatis.";
RL   Microbiology 148:3079-3087(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16194230; DOI=10.1111/j.1365-2958.2005.04847.x;
RA   Sonden B., Kocincova D., Deshayes C., Euphrasie D., Rhayat L., Laval F.,
RA   Frehel C., Daffe M., Etienne G., Reyrat J.M.;
RT   "Gap, a mycobacterial specific integral membrane protein, is required for
RT   glycolipid transport to the cell surface.";
RL   Mol. Microbiol. 58:426-440(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA   Shearer A.G., Altman T., Rhee C.D.;
RT   "Finding sequences for over 270 orphan enzymes.";
RL   PLoS ONE 9:E97250-E97250(2014).
CC   -!- FUNCTION: O-methyltransferase that modifies the hydroxy group of the
CC       fatty acids. Oleate is the most effective fatty acid acceptor.
CC       {ECO:0000269|PubMed:12368441}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a fatty acid + S-adenosyl-L-methionine = a fatty acid methyl
CC         ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:23012,
CC         ChEBI:CHEBI:4986, ChEBI:CHEBI:28868, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:59789; EC=2.1.1.15;
CC   -!- DISRUPTION PHENOTYPE: Cells are unable to methylate the
CC       glycopeptidolipid fatty acids. {ECO:0000269|PubMed:12368441}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABK70254.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AY138899; AAF05995.1; -; Genomic_DNA.
DR   EMBL; AY439015; ABB72073.1; -; Genomic_DNA.
DR   EMBL; CP000480; ABK70254.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CP001663; AFP36867.1; -; Genomic_DNA.
DR   RefSeq; WP_014876764.1; NZ_SIJM01000018.1.
DR   RefSeq; YP_884806.1; NC_008596.1.
DR   AlphaFoldDB; Q9RMN9; -.
DR   SMR; Q9RMN9; -.
DR   STRING; 246196.MSMEI_0386; -.
DR   EnsemblBacteria; ABK70254; ABK70254; MSMEG_0393.
DR   EnsemblBacteria; AFP36867; AFP36867; MSMEI_0386.
DR   GeneID; 66738580; -.
DR   KEGG; msg:MSMEI_0386; -.
DR   KEGG; msm:MSMEG_0393; -.
DR   PATRIC; fig|246196.19.peg.390; -.
DR   eggNOG; COG2226; Bacteria.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0030733; F:fatty acid O-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..274
FT                   /note="Fatty-acid O-methyltransferase"
FT                   /id="PRO_0000430256"
SQ   SEQUENCE   274 AA;  31353 MW;  41B8DD18ED0F67E1 CRC64;
     MALGNALVEA RDRVAWRLNI KVAQQAQKLV YRYATRRLKD DDVVFLNYGY EEDPPMGIPL
     SESDELNRYS IQLYHSTAAQ ADVEGKRVLE VGCGHGGGAS YLARTFRPAT YTGLDLNSDG
     INFCRRRHNI AGLEFVQGDA QDLPFPDKNF DAVLNVESSH LYPRFDVFLT EVARVLRPGG
     YFLYTDARPR YDIPEWERAL ADAPLQMLSQ RAINFEVVRG MEKNLDALES VVDRVAPALL
     RDWIQKYGPA RRAYEELREN TTEYRMYCFV KPAE