WBBL_MYCTU
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 03-AUG-2022, entry version 48.
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., 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 [2]
RP PROTEIN SEQUENCE OF 2-20, AND SEQUENCE REVISION TO N-TERMINUS.
RC STRAIN=H37Rv;
RX PubMed=34915127; DOI=10.1016/j.ygeno.2021.12.001;
RA Shi J., Meng S., Wan L., Zhang Z., Jiang S., Zhu H., Dai E., Chang L.,
RA Gao H., Wan K., Zhang L., Zhao X., Liu H., Lyu Z., Zhang Y., Xu P.;
RT "Deep N-terminomics of Mycobacterium tuberculosis H37Rv extensively correct
RT annotated encoding genes.";
RL Genomics 114:292-304(2021).
RN [3]
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 needed
RT for the formation of the arabinogalactan-peptidoglycan linker, leads to
RT irreversible loss of viability.";
RL J. Biol. Chem. 279:43540-43546(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 FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL 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 [6]
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: 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:0000269|PubMed:15294902,
CC ECO:0000269|PubMed:19047740}.
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 Evidence={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-trans,octacis-
CC 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 loss
CC of viability. {ECO:0000269|PubMed:15294902}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CCP46084.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000269|PubMed:34915127};
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DR EMBL; AL123456; CCP46084.1; ALT_INIT; Genomic_DNA.
DR PIR; B70978; B70978.
DR RefSeq; YP_177952.3; NC_000962.3.
DR AlphaFoldDB; P9WMY3; -.
DR SMR; P9WMY3; -.
DR STRING; 83332.Rv3265c; -.
DR PaxDb; P9WMY3; -.
DR DNASU; 888714; -.
DR GeneID; 888714; -.
DR KEGG; mtu:Rv3265c; -.
DR PATRIC; fig|83332.12.peg.3652; -.
DR TubercuList; Rv3265c; -.
DR eggNOG; COG1216; Bacteria.
DR BioCyc; MetaCyc:G185E-7539-MON; -.
DR BRENDA; 2.4.1.289; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0102096; F:decaprenyl-N-acetyl-alpha-D-glucosaminyl-pyrophosphate:dTDP-alpha-L-rhamnose rhamnosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IDA:UniProtKB.
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 Direct protein sequencing; Glycosyltransferase; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:34915127"
FT CHAIN 2..307
FT /note="N-acetylglucosaminyl-diphospho-decaprenol L-
FT rhamnosyltransferase"
FT /id="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
