ID   RNTF_MYCBP              Reviewed;         449 AA.
AC   A1KMV6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=PGL/p-HBAD biosynthesis rhamnosyltransferase;
DE            EC=2.4.1.-;
GN   OrderedLocusNames=BCG_2983c;
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).
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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 28 family.
CC       {ECO:0000305}.
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DR   EMBL; AM408590; CAL72972.1; -; Genomic_DNA.
DR   RefSeq; WP_003414922.1; NC_008769.1.
DR   AlphaFoldDB; A1KMV6; -.
DR   SMR; A1KMV6; -.
DR   CAZy; GT1; Glycosyltransferase Family 1.
DR   KEGG; mbb:BCG_2983c; -.
DR   HOGENOM; CLU_692271_0_0_11; -.
DR   OMA; WNIEECV; -.
DR   Proteomes; UP000001472; Chromosome.
DR   GO; GO:0016758; F:hexosyltransferase activity; IEA:UniProt.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..449
FT                   /note="PGL/p-HBAD biosynthesis rhamnosyltransferase"
FT                   /id="PRO_0000313791"
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