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GLFT1_MYCS2
ID   GLFT1_MYCS2             Reviewed;         302 AA.
AC   A0R5Z2; I7FMT0;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Galactofuranosyltransferase GlfT1 {ECO:0000305};
DE            Short=GalTr 1 {ECO:0000305};
DE            EC=2.4.1.287 {ECO:0000269|PubMed:18055597};
DE   AltName: Full=Arabinogalactan galactosyltransferase 1 {ECO:0000305};
DE   AltName: Full=Rhamnopyranosyl-N-acetylglucosaminyl-diphospho-decaprenol beta-1,4/1,5-galactofuranosyltransferase;
DE   AltName: Full=UDP-Galf:alpha-3-L-rhamnosyl-alpha-D-GlcNAc-pyrophosphate polyprenol, galactofuranosyl transferase;
GN   Name=glfT1 {ECO:0000303|PubMed:18055597};
GN   OrderedLocusNames=MSMEG_6367, MSMEI_6199;
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).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND SUBSTRATE SPECIFICITY.
RC   STRAIN=ATCC 700084 / mc(2)155;
RX   PubMed=18055597; DOI=10.1128/jb.01326-07;
RA   Belanova M., Dianiskova P., Brennan P.J., Completo G.C., Rose N.L.,
RA   Lowary T.L., Mikusova K.;
RT   "Galactosyl transferases in mycobacterial cell wall synthesis.";
RL   J. Bacteriol. 190:1141-1145(2008).
CC   -!- FUNCTION: Involved in the biosynthesis of the arabinogalactan (AG)
CC       region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an
CC       essential component of the mycobacterial cell wall. Catalyzes the
CC       transfer of the first two galactofuranosyl (Galf) units from UDP-
CC       galactofuranose (UDP-Galf) onto the rhamnosyl-GlcNAc-diphospho-
CC       decaprenol (Rha-GlcNAc-PP-C50) acceptor, yielding galactofuranosyl-
CC       galactofuranosyl-rhamnosyl-GlcNAc-diphospho-decaprenol (Galf-Galf-Rha-
CC       GlcNAc-PP-C50). Thus, GlfT1 is the initiator of galactan synthesis,
CC       while GlfT2 continues with the subsequent polymerization events.
CC       {ECO:0000269|PubMed:18055597}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-
CC         diphospho-trans,octa-cis-decaprenol + 2 UDP-alpha-D-galactofuranose =
CC         beta-D-galactofuranosyl-(1->5)-beta-D-galactofuranosyl-(1->4)-alpha-
CC         L-rhamnosyl-(1->3)-N-acetyl-alpha-D-glucosaminyl-diphospho-
CC         trans,octa-cis-decaprenol + 2 H(+) + 2 UDP; Xref=Rhea:RHEA:34379,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:66915,
CC         ChEBI:CHEBI:67209, ChEBI:CHEBI:67210; EC=2.4.1.287;
CC         Evidence={ECO:0000269|PubMed:18055597};
CC   -!- PATHWAY: Cell wall biogenesis; cell wall polysaccharide biosynthesis.
CC       {ECO:0000305|PubMed:18055597}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P9WMX3}.
CC       Secreted, cell wall {ECO:0000250|UniProtKB:P9WMX3}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AFP42625.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP000480; ABK69689.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP42625.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011731236.1; NZ_SIJM01000013.1.
DR   RefSeq; YP_890580.1; NC_008596.1.
DR   AlphaFoldDB; A0R5Z2; -.
DR   SMR; A0R5Z2; -.
DR   STRING; 246196.MSMEI_6199; -.
DR   CAZy; GT2; Glycosyltransferase Family 2.
DR   PRIDE; A0R5Z2; -.
DR   EnsemblBacteria; ABK69689; ABK69689; MSMEG_6367.
DR   EnsemblBacteria; AFP42625; AFP42625; MSMEI_6199.
DR   GeneID; 66737645; -.
DR   KEGG; msg:MSMEI_6199; -.
DR   KEGG; msm:MSMEG_6367; -.
DR   PATRIC; fig|246196.19.peg.6195; -.
DR   eggNOG; COG1216; Bacteria.
DR   OMA; RFYTYRN; -.
DR   OrthoDB; 865276at2; -.
DR   UniPathway; UPA00963; -.
DR   Proteomes; UP000000757; Chromosome.
DR   Proteomes; UP000006158; Chromosome.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0016740; F:transferase activity; IDA:UniProtKB.
DR   GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0044038; P:cell wall macromolecule biosynthetic process; IDA:UniProtKB.
DR   GO; GO:0071555; P:cell wall organization; IDA:UniProtKB.
DR   InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR   SUPFAM; SSF53448; SSF53448; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell wall; Cell wall biogenesis/degradation;
KW   Glycosyltransferase; Membrane; Reference proteome; Secreted; Transferase.
FT   CHAIN           1..302
FT                   /note="Galactofuranosyltransferase GlfT1"
FT                   /id="PRO_0000395357"
SQ   SEQUENCE   302 AA;  34041 MW;  407E1D4CA50DA4BD CRC64;
     MTHTEVVCAV VVTHRRRELL ATSLDAVVSQ DRKPDHLIVV DNDNDPQVRE LVTGQPVPST
     YLGSRRNLGG AGGFALGMLH ALALGADWIW LADDDGRPAD TTVLSTLLSC AHTHSLAEVS
     PMVCNLDDPQ RLAFPLRRGL VWRRLTSELR TDSSSSSGDL LPGIASLFNG ALFRADTVDA
     VGVPDLRLFV RGDEVELHRR LVRSGLPFGT CLTASYLHPC GTDEFKPILG GRMHTQYPDD
     ETKRFFTYRN RGYLLSQPGL RKLLPQEWLR FGWYFLVSRR DLAGLREWIR LRRLGRRERF
     QR
 
 
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