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GLFT2_MYCS2
ID   GLFT2_MYCS2             Reviewed;         646 AA.
AC   A0R628; I7GFR0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Galactofuranosyltransferase GlfT2 {ECO:0000250|UniProtKB:O53585};
DE            Short=GalTr 2 {ECO:0000250|UniProtKB:O53585};
DE            EC=2.4.1.288 {ECO:0000250|UniProtKB:O53585};
DE   AltName: Full=Arabinogalactan galactosyltransferase 2 {ECO:0000250|UniProtKB:O53585};
DE   AltName: Full=Galactofuranosylgalactofuranosylrhamnosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,5/1,6-galactofuranosyltransferase {ECO:0000250|UniProtKB:O53585};
DE   AltName: Full=Polymerizing galactofuranosyltransferase GlfT2 {ECO:0000250|UniProtKB:O53585};
GN   Name=glfT2 {ECO:0000250|UniProtKB:O53585};
GN   OrderedLocusNames=MSMEG_6403, MSMEI_6235;
OS   Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS   smegmatis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=246196;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RA   Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA   Fraser C.M.;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA   Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA   Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT   "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT   mutations or sequencing errors?";
RL   Genome Biol. 8:R20.1-R20.9(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18955433; DOI=10.1101/gr.081901.108;
RA   Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA   Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT   "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT   and a new MS-based protocol.";
RL   Genome Res. 19:128-135(2009).
CC   -!- FUNCTION: Involved in the galactan polymerization of the
CC       arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan
CC       (mAGP) complex, an essential component of the mycobacteria cell wall.
CC       Thus, successively transfers approximately 28 galactofuranosyl (Galf)
CC       residues from UDP-galactofuranose (UDP-Galf) onto the galactofuranosyl-
CC       galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-
CC       GlcNAc-PP-C50) acceptor produced by GlfT1, with alternating 1->5 and
CC       1->6 links, forming a galactan domain with approximately 30
CC       galactofuranosyl residues. {ECO:0000250|UniProtKB:O53585}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-
CC         alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC         trans,octa-cis-decaprenol + 28 UDP-alpha-D-galactofuranose = [beta-D-
CC         galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->6)]14-beta-D-
CC         galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-L-
CC         rhamnopyranosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC         trans,octa-cis-decaprenol + 28 H(+) + 28 UDP; Xref=Rhea:RHEA:34391,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915,
CC         ChEBI:CHEBI:67210, ChEBI:CHEBI:67212; EC=2.4.1.288;
CC         Evidence={ECO:0000250|UniProtKB:O53585};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000250|UniProtKB:O53585};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:O53585};
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC       {ECO:0000250|UniProtKB:O53585}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:O53585}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O53585}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
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DR   EMBL; CP000480; ABK72427.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42661.1; -; Genomic_DNA.
DR   RefSeq; WP_011731265.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890616.1; NC_008596.1.
DR   AlphaFoldDB; A0R628; -.
DR   SMR; A0R628; -.
DR   STRING; 246196.MSMEI_6235; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; A0R628; -.
DR   EnsemblBacteria; ABK72427; ABK72427; MSMEG_6403.
DR   EnsemblBacteria; AFP42661; AFP42661; MSMEI_6235.
DR   GeneID; 66737680; -.
DR   KEGG; msg:MSMEI_6235; -.
DR   KEGG; msm:MSMEG_6403; -.
DR   PATRIC; fig|246196.19.peg.6229; -.
DR   eggNOG; COG1216; Bacteria.
DR   OMA; NGWWMCL; -.
DR   OrthoDB; 865276at2; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; ISS:UniProtKB.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044038; P:cell wall macromolecule biosynthetic process; ISS:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; ISS:UniProtKB.
DR   InterPro; IPR045699; GlfT2_C.
DR   InterPro; IPR040492; GlfT2_N.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   Pfam; PF19320; GlfT2_domain3; 1.
DR   Pfam; PF17994; Glft2_N; 1.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Cell wall biogenesis/degradation; Glycosyltransferase;
KW   Magnesium; Manganese; Membrane; Metal-binding; Reference proteome;
KW   Transferase.
FT   CHAIN           1..646
FT                   /note="Galactofuranosyltransferase GlfT2"
FT                   /id="PRO_0000395358"
FT   ACT_SITE        384
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         182
FT                   /ligand="UDP-alpha-D-galactofuranose"
FT                   /ligand_id="ChEBI:CHEBI:66915"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         211
FT                   /ligand="UDP-alpha-D-galactofuranose"
FT                   /ligand_id="ChEBI:CHEBI:66915"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         240
FT                   /ligand="UDP-alpha-D-galactofuranose"
FT                   /ligand_id="ChEBI:CHEBI:66915"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         267
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         267
FT                   /ligand="UDP-alpha-D-galactofuranose"
FT                   /ligand_id="ChEBI:CHEBI:66915"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         269
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
FT   BINDING         408
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250|UniProtKB:O53585"
SQ   SEQUENCE   646 AA;  71573 MW;  58E7858070950B59 CRC64;
     MSDIPSGALE ADESRAVSLL SRVILPRPGE PLDVRKLYIE ESTTNSRRAH APTRTSLEIG
     PESEVSFATY FNAFPASYWR RWSTLDTVVL RVELTGTARV DVYRSKATGA RITVGGAPVA
     GEGDGPAAVE FEIDLTPFED GGWIWFDITT NTAVRVHSAG WYAPVPAPGR ANVAVGIPTF
     NRPADCVNAL AALTSDPLVD EVISAVIVSD QGTSKAKDHP GFADAAARLG DRLSIHNQPN
     LGGSGGYSRV MYEALKNTDC EQILFMDDDI RIEPDSILRA LAMNRFAKSP ILVGGQMLNL
     QEPSHLHVMG EVVDRANFMW TAAPNAEYDH DFAKFKLSDA EEPRTKLLHR RVDVDFNGWW
     MCMIPRQIAE ELGQPLPLFI KWDDAEYGLR AGEHGYGTVT LPGAAIWHMA WSDKDDAIDW
     QAYFHLRNRL VVAALHWDGP VSGLIASHLK ATIKHLLCLE YSTVAIQNKA MEDFLAGPEN
     LFSILESAMP DVRKLRSQYP DAVVLPGATS LPPASDMRRK KIAIPVSKPA IAVNLARGVV
     HQLRSHDPET HVRPQINVAT QDARWFSLCR VDGVTVTTAD GRGVVYRQRD RAKMFALLRA
     SLRQQARLAR KFDRMRKVYR DALPMLTSTQ KWESVLLTET PEKVGR
 
 
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