ID   WBBL_MYCTO              Reviewed;         307 AA.
AC   P9WMY2; L0TF42; Q6MWZ0; Q7D5T2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   25-MAY-2022, entry version 34.
DE   RecName: Full=N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase;
DE            EC=2.4.1.289;
DE   AltName: Full=Rhamnosyltransferase WbbL;
DE   AltName: Full=dTDP-Rha:alpha-D-GlcNAc-pyrophosphate polyprenol, alpha-3-L-rhamnosyltransferase;
GN   Name=wbbL; Synonyms=wbbL1; OrderedLocusNames=MT3365;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of the mycolylarabinogalactan-
CC       peptidoglycan (mAGP) complex, an essential component of the
CC       mycobacterial cell wall. Catalyzes the transfer of the rhamnosyl moiety
CC       from dTDP-rhamnosyl (dTDP-Rha) onto the decaprenyl-pyrophosphoryl-
CC       GlcNAc (C50-PP-GlcNAc), yielding rhamnosyl-decaprenyl-pyrophosphoryl-
CC       GlcNAc (Rha-C50-PP-GlcNAc). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP-beta-L-rhamnose + N-acetyl-alpha-D-glucosaminyl-1-
CC         diphospho-trans,octa-cis-decaprenol = alpha-L-rhamnosyl-(1->3)-N-
CC         acetyl-alpha-D-glucosaminyl-diphospho-trans,octa-cis-decaprenol +
CC         dTDP + H(+); Xref=Rhea:RHEA:34487, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57510, ChEBI:CHEBI:58369, ChEBI:CHEBI:65080,
CC         ChEBI:CHEBI:67209; EC=2.4.1.289;
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK47706.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK47706.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70978; B70978.
DR   AlphaFoldDB; P9WMY2; -.
DR   SMR; P9WMY2; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   EnsemblBacteria; AAK47706; AAK47706; MT3365.
DR   KEGG; mtc:MT3365; -.
DR   HOGENOM; CLU_023845_0_0_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0102096; F:decaprenyl-N-acetyl-alpha-D-glucosaminyl-pyrophosphate:dTDP-alpha-L-rhamnose rhamnosyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..307
FT                   /note="N-acetylglucosaminyl-diphospho-decaprenol L-
FT                   rhamnosyltransferase"
FT                   /id="PRO_0000427222"
SQ   SEQUENCE   307 AA;  33920 MW;  6C3621E158BB096D CRC64;
     MTDVLPVVAV TYSPGPHLER FLASLSLATE RPVSVLLADN GSTDGTPQAA VQRYPNVRLL
     PTGANLGYGT AVNRTIAQLG EMAGDAGEPW VDDWVIVANP DVQWGPGSID ALLDAASRWP
     RAGALGPLIR DPDGSVYPSA RQMPSLIRGG MHAVLGPFWP RNPWTTAYRQ ERLEPSERPV
     GWLSGSCLLV RRSAFGQVGG FDERYFMYME DVDLGDRLGK AGWLSVYVPS AEVLHHKAHS
     TGRDPASHLA AHHKSTYIFL ADRHSGWWRA PLRWTLRGSL ALRSHLMVRS SLRRSRRRKL
     KLVEGRH