ID   RNTF_MYCTU              Reviewed;         449 AA.
AC   P9WN09; L0TBE0; P95130; Q50455; Q50456; Q7D6C8;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=PGL/p-HBAD biosynthesis rhamnosyltransferase;
DE            EC=2.4.1.-;
GN   OrderedLocusNames=Rv2962c;
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 RHAMNOSYLTRANSFERASE.
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=15292272; DOI=10.1074/jbc.m406246200;
RA   Perez E., Constant P., Lemassu A., Laval F., Daffe M., Guilhot C.;
RT   "Characterization of three glycosyltransferases involved in the
RT   biosynthesis of the phenolic glycolipid antigens from the Mycobacterium
RT   tuberculosis complex.";
RL   J. Biol. Chem. 279:42574-42583(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 transfer of the first rhamnosyl residue on p-
CC       hydroxybenzoic acid or phenolphthiocerol derivatives to form, after O-
CC       methylation at position 2 of the sugar unit, mono-O-methyl-glycosyl-p-
CC       hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-rhamnosyl-
CC       phenolphthiocerol dimycocerosate (also called mycoside B) during p-
CC       hydroxybenzoic acid derivatives (p-HBAD) and glycosylated
CC       phenolphthiocerol dimycocerosates (PGL) biosynthesis.
CC       {ECO:0000269|PubMed:15292272}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50942.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA50943.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00024; AAA50942.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; U00024; AAA50943.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL123456; CCP45766.1; -; Genomic_DNA.
DR   PIR; G70670; G70670.
DR   RefSeq; NP_217478.1; NC_000962.3.
DR   RefSeq; WP_003414922.1; NZ_NVQJ01000015.1.
DR   AlphaFoldDB; P9WN09; -.
DR   SMR; P9WN09; -.
DR   STRING; 83332.Rv2962c; -.
DR   PaxDb; P9WN09; -.
DR   DNASU; 887892; -.
DR   GeneID; 887892; -.
DR   KEGG; mtu:Rv2962c; -.
DR   PATRIC; fig|83332.111.peg.3300; -.
DR   TubercuList; Rv2962c; -.
DR   eggNOG; COG1819; Bacteria.
DR   OMA; WNIEECV; -.
DR   PhylomeDB; P9WN09; -.
DR   BioCyc; MetaCyc:G185E-7216-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:MTBBASE.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..449
FT                   /note="PGL/p-HBAD biosynthesis rhamnosyltransferase"
FT                   /id="PRO_0000313792"
SQ   SEQUENCE   449 AA;  49433 MW;  205FDB0855C0A109 CRC64;
     MRVSCVYATA SRWGGPPVAS EVRGDAAIST TPDAAPGLAA RRRRILFVAE AVTLAHVVRP
     FALAQSLDPS RYEVHFACDP RYNQLLGPLP FRHHAIHTIP SERFFGNLTQ GRFYAMRTLR
     KYVEADLRVL DEIAPDLVVG DLRISLSVSA RLAGIPYIAI ANAYWSPYAQ RRFPLPDVIW
     TRLFGVRLVK LLYRLERPLL FALQCMPLNW VRRRHGLSSL GWNLCRIFTD GDHTLYADVP
     ELMPTYDLPA NHEYLGPVLW SPAGKPPTWW DSLPTDRPIV YATLGTSGGR NLLQLVLNAL
     AELPVTVIAA TAGRSDLKTV PANAFVADYL PGEAAAARSA VVVCNGGSLT TQQALVAGVP
     VIGVAGNLDQ HLNMEAVERA GAGVLLRTER LKSQRVAGAV MQVISRSEYR QAAARLADAF
     GRDRVGFPQH VENALRLMPE NRPRTWLAS