ID   WBBL_MYCTU              Reviewed;         307 AA.
AC   P9WMY3; L0TF42; Q6MWZ0; Q7D5T2;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2016, sequence version 2.
DT   15-FEB-2017, entry version 21.
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=Rv3265c;
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 [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.,
RA   Harris D.E., Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III,
RA   Tekaia F., Badcock K., Basham D., Brown D., Chillingworth T.,
RA   Connor R., Davies R.M., Devlin K., Feltwell T., Gentles S., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Krogh A., McLean J., Moule S.,
RA   Murphy L.D., Oliver S., Osborne J., Quail M.A., Rajandream M.A.,
RA   Rogers J., Rutter S., Seeger K., Skelton S., Squares S., Squares R.,
RA   Sulston J.E., Taylor K., Whitehead S., Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the
RT   complete genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   FUNCTION AS A RHAMNOSYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RX   PubMed=15294902; DOI=10.1074/jbc.M407782200;
RA   Mills J.A., Motichka K., Jucker M., Wu H.P., Uhlik B.C., Stern R.J.,
RA   Scherman M.S., Vissa V.D., Pan F., Kundu M., Ma Y.F., McNeil M.;
RT   "Inactivation of the mycobacterial rhamnosyltransferase, which is
RT   needed for the formation of the arabinogalactan-peptidoglycan linker,
RT   leads to irreversible loss of viability.";
RL   J. Biol. Chem. 279:43540-43546(2004).
RN   [3]
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
RT   tuberculosis through an interactome, reactome and genome-scale
RT   structural analysis.";
RL   BMC Syst. Biol. 2:109-109(2008).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=19047740; DOI=10.1099/mic.0.2008/023366-0;
RA   Grzegorzewicz A.E., Ma Y., Jones V., Crick D., Liav A., McNeil M.R.;
RT   "Development of a microtitre plate-based assay for lipid-linked
RT   glycosyltransferase products using the mycobacterial cell wall
RT   rhamnosyltransferase WbbL.";
RL   Microbiology 154:3724-3730(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.,
RA   Yadav A.K., Shrivastava P., Marimuthu A., Anand S., Sundaram H.,
RA   Kingsbury R., Harsha H.C., Nair B., Prasad T.S., Chauhan D.S.,
RA   Katoch K., Katoch V.M., Kumar P., Chaerkady R., Ramachandran S.,
RA   Dash D., Pandey A.;
RT   "Proteogenomic analysis of Mycobacterium tuberculosis by high
RT   resolution mass spectrometry.";
RL   Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC   -!- FUNCTION: Involved in the biosynthesis of the
CC       mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential
CC       component of the mycobacterial cell wall. Catalyzes the transfer
CC       of the rhamnosyl moiety from dTDP-rhamnosyl (dTDP-Rha) onto the
CC       decaprenyl-pyrophosphoryl-GlcNAc (C50-PP-GlcNAc), yielding
CC       rhamnosyl-decaprenyl-pyrophosphoryl-GlcNAc (Rha-C50-PP-GlcNAc).
CC       {ECO:0000269|PubMed:15294902, ECO:0000269|PubMed:19047740}.
CC   -!- CATALYTIC ACTIVITY: dTDP-6-deoxy-beta-L-mannose + N-acetyl-alpha-
CC       D-glucosaminyl-diphospho-trans,octacis-decaprenol = dTDP + alpha-
CC       L-rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC       trans,octacis-decaprenol. {ECO:0000269|PubMed:19047740}.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:19047740};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:19047740};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=18 uM for N-acetyl-alpha-D-glucosaminyl-diphospho-
CC         trans,octacis-decaprenol {ECO:0000269|PubMed:19047740};
CC         KM=35 uM for dTDP-6-deoxy-beta-L-mannose
CC         {ECO:0000269|PubMed:19047740};
CC       pH dependence:
CC         Optimum pH is 8.6. {ECO:0000269|PubMed:19047740};
CC       Temperature dependence:
CC         Optimum temperature is 30 degrees Celsius.
CC         {ECO:0000269|PubMed:19047740};
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene lead to irreversible
CC       loss of viability. {ECO:0000269|PubMed:15294902}.
CC   -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CCP46084.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305|PubMed:21969609};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AL123456; CCP46084.1; ALT_INIT; Genomic_DNA.
DR   PIR; B70978; B70978.
DR   RefSeq; WP_003899992.1; NZ_KK339370.1.
DR   RefSeq; WP_003901582.1; NC_000962.3.
DR   RefSeq; YP_177952.3; NC_000962.3.
DR   ProteinModelPortal; P9WMY3; -.
DR   STRING; 83332.Rv3265c; -.
DR   PaxDb; P9WMY3; -.
DR   EnsemblBacteria; CCP46084; CCP46084; Rv3265c.
DR   GeneID; 888714; -.
DR   KEGG; mtu:Rv3265c; -.
DR   TubercuList; Rv3265c; -.
DR   eggNOG; ENOG4105F3Q; Bacteria.
DR   eggNOG; COG1216; LUCA.
DR   KO; K16870; -.
DR   OMA; FFIVANP; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IDA:MTBBASE.
DR   GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IMP:MTBBASE.
DR   GO; GO:0040007; P:growth; IMP:MTBBASE.
DR   Gene3D; 3.90.550.10; -; 1.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Glycosyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN         1    307       N-acetylglucosaminyl-diphospho-decaprenol
FT                                L-rhamnosyltransferase.
FT                                /FTId=PRO_0000395354.
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
//