ID   RNMT_MYCTU              Reviewed;         245 AA.
AC   P9WIM5; L0TDW5; O08024; Q50457; Q798M6; Q7D6D0;
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=Rhamnosyl O-methyltransferase;
DE            EC=2.1.1.-;
DE   Flags: Precursor;
GN   OrderedLocusNames=Rv2959c;
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 [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (SEP-1994) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
RP   FUNCTION AS METHYLTRANSFERASE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15292265; DOI=10.1074/jbc.m406134200;
RA   Perez E., Constant P., Laval F., Lemassu A., Laneelle M.-A., Daffe M.,
RA   Guilhot C.;
RT   "Molecular dissection of the role of two methyltransferases in the
RT   biosynthesis of phenolglycolipids and phthiocerol dimycoserosate in the
RT   Mycobacterium tuberculosis complex.";
RL   J. Biol. Chem. 279:42584-42592(2004).
RN   [4]
RP   IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX   PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA   Raman K., Yeturu K., Chandra N.;
RT   "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT   through an interactome, reactome and genome-scale structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [5]
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).
CC   -!- FUNCTION: Catalyzes the O-methylation of the hydroxyl group located on
CC       C-2 of the first rhamnosyl residue linked to the phenolic group of
CC       glycosylated phenolphthiocerol dimycocerosates (PGL) and p-
CC       hydroxybenzoic acid derivatives (p-HBAD).
CC       {ECO:0000269|PubMed:15292265}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the rhamnosyl O-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; U00024; AAA50941.1; -; Genomic_DNA.
DR   EMBL; AL123456; CCP45763.1; -; Genomic_DNA.
DR   PIR; D70670; D70670.
DR   RefSeq; NP_217475.1; NC_000962.3.
DR   RefSeq; WP_003414919.1; NZ_NVQJ01000015.1.
DR   AlphaFoldDB; P9WIM5; -.
DR   SMR; P9WIM5; -.
DR   STRING; 83332.Rv2959c; -.
DR   PaxDb; P9WIM5; -.
DR   DNASU; 887862; -.
DR   GeneID; 45426947; -.
DR   GeneID; 887862; -.
DR   KEGG; mtu:Rv2959c; -.
DR   PATRIC; fig|83332.111.peg.3298; -.
DR   TubercuList; Rv2959c; -.
DR   eggNOG; COG3510; Bacteria.
DR   OMA; MIQGSSI; -.
DR   BioCyc; MetaCyc:G185E-7213-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0030206; P:chondroitin sulfate biosynthetic process; IMP:MTBBASE.
DR   GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IMP:MTBBASE.
DR   GO; GO:0008610; P:lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR007072; Rhamnosyl_O-MeTrfase_CmcI.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF04989; CmcI; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
PE   1: Evidence at protein level;
KW   Lipid biosynthesis; Lipid metabolism; Methyltransferase;
KW   Reference proteome; Signal; Transferase.
FT   SIGNAL          1..38
FT                   /evidence="ECO:0000255"
FT   CHAIN           39..245
FT                   /note="Rhamnosyl O-methyltransferase"
FT                   /id="PRO_0000305181"
SQ   SEQUENCE   245 AA;  27845 MW;  0B2540CBB532E3A6 CRC64;
     MGLVWRSRTS LVGQLIGLVR LVASFAAQLF YRPSDAVAEE YHKWYYGNLV WTKTTYMGIN
     CWKSVSDMWN YQEILSELQP SLVIEFGTRY GGSAVYFANI MRQIGQPFKV LTVDNSHKAL
     DPRARREPDV LFVESSSTDP AIAEQIQRLK NEYPGKIFAI LDSDHSMNHV LAEMKLLRPL
     LSAGDYLVVE DSNINGHPVL PGFGPGPYEA IEAYEDEFPN DYKHDAEREN KFGWTSAPNG
     FLIRN