GLTR1_MYCTU
ID GLTR1_MYCTU Reviewed; 256 AA.
AC P9WMX7; L0TBD5; P0A599; Q50459;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=PGL/p-HBAD biosynthesis glycosyltransferase Rv2957;
DE EC=2.4.1.-;
GN OrderedLocusNames=Rv2957; ORFNames=MTCY349.31c, u0002kc;
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 GLYCOSYLTRANSFERASE.
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: Involved in glycosylation steps downstream of mono-O-methyl-
CC glycosyl-p-hydroxybenzoic acid derivative (p-HBAD I) and 2-O-methyl-
CC rhamnosyl-phenolphthiocerol dimycocerosate (mycoside B) during the 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 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA50938.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CCP45761.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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; U00024; AAA50938.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL123456; CCP45761.1; ALT_INIT; Genomic_DNA.
DR PIR; B70670; B70670.
DR RefSeq; NP_217473.1; NC_000962.3.
DR AlphaFoldDB; P9WMX7; -.
DR SMR; P9WMX7; -.
DR STRING; 83332.Rv2957; -.
DR PaxDb; P9WMX7; -.
DR DNASU; 887258; -.
DR GeneID; 887258; -.
DR KEGG; mtu:Rv2957; -.
DR PATRIC; fig|83332.12.peg.3297; -.
DR TubercuList; Rv2957; -.
DR eggNOG; COG0463; Bacteria.
DR OMA; SADFDWC; -.
DR BioCyc; MetaCyc:G185E-7211-MON; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016757; F:glycosyltransferase activity; IBA:GO_Central.
DR GO; GO:0016758; F:hexosyltransferase activity; IDA:MTBBASE.
DR GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR001173; Glyco_trans_2-like.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF00535; Glycos_transf_2; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..256
FT /note="PGL/p-HBAD biosynthesis glycosyltransferase Rv2957"
FT /id="PRO_0000059251"
SQ SEQUENCE 256 AA; 29013 MW; 90C6EC628C59CA57 CRC64;
MAAPMFSIII PTLNVAAVLP ACLDSIARQT CGDFELVLVD GGSTDETLDI ANIFAPNLGE
RLIIHRDTDQ GVYDAMNRGV DLATGTWLLF LGADDSLYEA DTLARVAAFI GEHEPSDLVY
GDVIMRSTNF RWGGAFDLDR LLFKRNICHQ AIFYRRGLFG TIGPYNLRYR VLADWDFNIR
CFSNPALVTR YMHVVVASYN EFGGLSNTIV DKEFLKRLPM STRLGIRLVI VLVRRWPKVI
SRAMVMRTVI SWRRRR