GTFB_STRAG
ID GTFB_STRAG Reviewed; 442 AA.
AC Q3S2Y1;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 25-MAY-2022, entry version 43.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB {ECO:0000255|HAMAP-Rule:MF_01473};
DE AltName: Full=Glycosyltransferase chaperone Gtf2;
DE AltName: Full=Glycosyltransferase stabilizing protein GtfB {ECO:0000255|HAMAP-Rule:MF_01473};
DE AltName: Full=Glycosyltransferase-stabilizing protein Gtf2 {ECO:0000303|PubMed:21862581};
GN Name=gtfB {ECO:0000255|HAMAP-Rule:MF_01473};
GN Synonyms=gtf2 {ECO:0000303|PubMed:21862581};
OS Streptococcus agalactiae.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1311;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=J48;
RX PubMed=16549667; DOI=10.1099/mic.0.28516-0;
RA Seifert K.N., Adderson E.E., Whiting A.A., Bohnsack J.F., Crowley P.J.,
RA Brady L.J.;
RT "A unique serine-rich repeat protein (Srr-2) and novel surface antigen
RT (epsilon) associated with a virulent lineage of serotype III Streptococcus
RT agalactiae.";
RL Microbiology 152:1029-1040(2006).
RN [2]
RP FUNCTION AS A STABILIZING PROTEIN, PATHWAY, INTERACTION WITH GTFA (GTF1),
RP EXPRESSION IN S.PARASANGUIS, AND DISRUPTION PHENOTYPE.
RC STRAIN=J48;
RX PubMed=21862581; DOI=10.1074/jbc.m111.239350;
RA Wu R., Wu H.;
RT "A molecular chaperone mediates a two-protein enzyme complex and
RT glycosylation of serine-rich streptococcal adhesins.";
RL J. Biol. Chem. 286:34923-34931(2011).
CC -!- FUNCTION: Required for the polymorphic O-glycosylation of the serine-
CC rich repeat protein Srr2. A stabilizing protein that is part of the
CC accessory SecA2/SecY2 system specifically required to export serine-
CC rich repeat proteins, probably Srr2 in this organism. The GtfA-GtfB
CC (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-GlcNAc to
CC Srr2 substrate, attaching the first sugar residue. Stabilizes the
CC glycosylation activity of GtfA in vivo. Upon expression in a gtfB
CC deletion mutant of S.parasanguis, GtfB confers incorrect glycosylation
CC and partial complementation of a biofilm formation defect, while
CC GtfA/GtfB restores correct expression of serine-rich repeat protein
CC Fap1 and completely restores a biofilm formation defect in a
CC S.parasanguis double gtfA-gtfB deletion. {ECO:0000269|PubMed:21862581}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:21862581}.
CC -!- SUBUNIT: Interacts with glycosyltransferase GtfA (Gtf1)
CC (PubMed:21862581). Interacts with glycosyltransferase GtfA; probably
CC forms a heterotetramer with 2 subunits each of GtfA and GtfB. Part of
CC the accessory SecA2/SecY2 protein translocation apparatus.
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:21862581}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
CC -!- DISRUPTION PHENOTYPE: No glycosylation of serine-rich repeat protein
CC Srr-2. {ECO:0000269|PubMed:21862581}.
CC -!- SIMILARITY: Belongs to the GtfB family. {ECO:0000305}.
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DR EMBL; DQ174691; AAZ95533.1; -; Genomic_DNA.
DR RefSeq; WP_000584700.1; NZ_VYQU01000016.1.
DR AlphaFoldDB; Q3S2Y1; -.
DR SMR; Q3S2Y1; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
DR GeneID; 66886244; -.
DR PATRIC; fig|1311.132.peg.1279; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IDA:UniProtKB.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0031647; P:regulation of protein stability; IMP:UniProtKB.
DR HAMAP; MF_01473; GtfB; 1.
DR InterPro; IPR014268; GtfB.
DR TIGRFAMs; TIGR02919; TIGR02919; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane.
FT CHAIN 1..442
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase stabilizing protein GtfB"
FT /id="PRO_0000418641"
SQ SEQUENCE 442 AA; 52552 MW; 0D05F27EA31F763F CRC64;
MIILFDFFDK KSKDLYYSLI TSGLHGNAVV INDDGFLPQN INSPYSFFCN MEGKNGNPLY
FNQVPLPDLW EIKGNNIEAE IWDFSIKRAK IFYQEPKYKR QVKNIDWFDN NKKVRYTDHY
NRFGWCFART HFDKNQNVTT KSYFDKDGKE VIVENFRTGV IILNWLNKDY FFDNRVAFLN
FYFSLMGWNL SRIWYNSLST PFFVSYRMTY PGEDILFWQE DIEDTIPANM RVLLESTNTR
TQKVIVQKKN TYHKIKSMLP KEQQEKIGYL GFIYPNKKNN KGRKDIFILT NSDQIEHLEV
LVHHLSDYHF HIAAYTEMSF KLMSFSQEQN VTLYPNISRT DLDNLFEICD IYFDINHGNE
VDDVIRRAFE YNHLIFAFDN TCHNRELVLD SNIISHTTCE QLINLMKNLS GSIMYLLEQQ
REQTSNETKE RYKEILGGYG NA