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GLTR2_MYCTU
ID   GLTR2_MYCTU             Reviewed;         428 AA.
AC   P9WFR1; L0TE23; P95134; Q50458; Q7D6D1;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=PGL/p-HBAD biosynthesis glycosyltransferase Rv2958c;
DE            EC=2.4.1.-;
GN   OrderedLocusNames=Rv2958c;
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 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   -!- SIMILARITY: Belongs to the UDP-glycosyltransferase family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA50940.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; U00024; AAA50940.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; AL123456; CCP45762.1; -; Genomic_DNA.
DR   PIR; C70670; C70670.
DR   RefSeq; NP_217474.1; NC_000962.3.
DR   RefSeq; WP_003899557.1; NZ_NVQJ01000015.1.
DR   AlphaFoldDB; P9WFR1; -.
DR   SMR; P9WFR1; -.
DR   STRING; 83332.Rv2958c; -.
DR   PaxDb; P9WFR1; -.
DR   DNASU; 887816; -.
DR   GeneID; 45426946; -.
DR   GeneID; 887816; -.
DR   KEGG; mtu:Rv2958c; -.
DR   TubercuList; Rv2958c; -.
DR   eggNOG; COG1819; Bacteria.
DR   OMA; THTEREY; -.
DR   PhylomeDB; P9WFR1; -.
DR   BioCyc; MetaCyc:G185E-7212-MON; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR   GO; GO:0016758; F:hexosyltransferase activity; IDA:MTBBASE.
DR   GO; GO:0008194; F:UDP-glycosyltransferase activity; IEA:InterPro.
DR   GO; GO:0009247; P:glycolipid biosynthetic process; IMP:MTBBASE.
DR   CDD; cd03784; GT1_Gtf-like; 1.
DR   InterPro; IPR002213; UDP_glucos_trans.
DR   Pfam; PF00201; UDPGT; 1.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..428
FT                   /note="PGL/p-HBAD biosynthesis glycosyltransferase Rv2958c"
FT                   /id="PRO_0000314436"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        328
FT                   /note="S -> L (in Ref. 1; AAA50940)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   428 AA;  46796 MW;  9AED70A49571BEF2 CRC64;
     MEETSVAGDP GPDAGTSTAP NAAPEPVARR QRILFVGEAA TLAHVVRPFV LARSLDPSRY
     EVHFACDPRF NKLLGPLPFP HHPIHTVPSE EVLLKIAQGR LFYNTRTLRK YIAADRKILN
     EIAPDVVVGD NRLSLSVSAR LAGIPYIAIA NAYWSPQARR RFPLPDVPWT RFFGVRPVSI
     LYRLYRPLIF ALYCLPLNWL RRKHGLSSLG WDLCRIFTDG DYTLYADVPE LVPTYNLPAN
     HRYLGPVLWS PDVKPPTWWH SLPTDRPIIY ATLGSSGGKN LLQVVLNALA DLPVTVIAAT
     AGRNHLKNVP ANAFVADYLP GEAAAARSAV VLCNGGSPTT QQALAAGVPV IGLPSNMDQH
     LNMEALERAG AGVLLRTERL NTEGVAAAVK QVLSGAEFRQ AARRLAEAFG PDFAGFPQHI
     ESALRLVC
 
 
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