GTFA_STRAG
ID GTFA_STRAG Reviewed; 506 AA.
AC Q3S2Y2;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase GtfA subunit {ECO:0000255|HAMAP-Rule:MF_01472};
DE EC=2.4.1.- {ECO:0000255|HAMAP-Rule:MF_01472};
DE AltName: Full=Glycosyltransferase Gtf1 {ECO:0000303|PubMed:21862581};
DE AltName: Full=Glycosyltransferase GtfA {ECO:0000255|HAMAP-Rule:MF_01472};
GN Name=gtfA {ECO:0000255|HAMAP-Rule:MF_01472};
GN Synonyms=gtf1 {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 GLYCOSYLTRANSFERASE, PATHWAY, INTERACTION WITH GTFB (GTF2),
RP AND EXPRESSION IN S.PARASANGUIS.
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 polymorphic O-glycosylation of the serine-rich
CC repeat protein Srr2. Catalyzes the first step in glycosylation by
CC transferring N-acetylglucosamine from UDP-GlcNAc to serine residues of
CC Srr2. Part of the accessory SecA2/SecY2 system specifically required to
CC export serine-rich repeat proteins, probably Srr2 in this organism. The
CC GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-
CC GlcNAc to Srr2 substrate. This subunit has low glycosyltransferase
CC activity; GtfB enhances glycosyltransferase activity in vitro. Upon
CC expression in S.parasanguis GtfA/GtfB restores expression of serine-
CC rich repeat protein Fap1 and complements a biofilm formation defect.
CC {ECO:0000269|PubMed:21862581}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-[N-
CC acetyl-alpha-D-glucosaminyl]-L-seryl-[protein] + H(+) + UDP;
CC Xref=Rhea:RHEA:59872, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:15471,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:143279; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01472};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}.
CC -!- SUBUNIT: Interacts with stabilizing protein GtfB (Gtf2), probably as a
CC heterotetramer with 2 subunits each of GtfA and GtfB, part of the
CC accessory SecA2/SecY2 protein translocation apparatus.
CC {ECO:0000269|PubMed:21862581}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472}. Cell
CC membrane {ECO:0000255|HAMAP-Rule:MF_01472}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01472}. Note=Cell membrane association
CC requires GtfB. {ECO:0000255|HAMAP-Rule:MF_01472}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_01472,
CC 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; DQ174691; AAZ95532.1; -; Genomic_DNA.
DR RefSeq; WP_000262050.1; NZ_VYQU01000016.1.
DR AlphaFoldDB; Q3S2Y2; -.
DR SMR; Q3S2Y2; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR PRIDE; Q3S2Y2; -.
DR GeneID; 66886245; -.
DR KEGG; sagg:EN73_06800; -.
DR PATRIC; fig|1311.132.peg.1280; -.
DR UniPathway; UPA00378; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0018242; P:protein O-linked glycosylation via serine; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01472; GtfA; 1.
DR InterPro; IPR001296; Glyco_trans_1.
DR InterPro; IPR014267; GtfA.
DR Pfam; PF00534; Glycos_transf_1; 1.
DR TIGRFAMs; TIGR02918; TIGR02918; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cytoplasm; Glycosyltransferase; Membrane;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..506
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase GtfA subunit"
FT /id="PRO_0000418643"
FT BINDING 16..19
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 241
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 384..385
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 404..407
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
SQ SEQUENCE 506 AA; 58196 MW; CD3AAD43E6BA40DF CRC64;
MVVYNLNRGI GWASSGVEYA QAYRSEVFRK LGVEAKFIFT DMFQNENIEH LTRNIGFEDN
EIIWLYTFFT DLTIAATSYS LQQLKESFSL PIDRTEKNGK IISFFFKGSS IVVTVMLNDE
SSNIVQRVEY LMGGKLVRKD YYSYTKMFSE YYAPEDIGPC LYQRTFYNED GSVAYEENVD
GENSIFKFKE TILYSKEELV GYMLEKLQLT NSDLILLDRS TGIGQAVLRN KGNAKVAVVV
HAEHYNVSAT DETTILWNNY YDYQFSNADS IDAFITSTET QTKTLIDQFK KYLNIEPVVY
TIPVGSLSKL QRKEWHERKA FSLLTCSRLA SEKHIDWLIN AVVEANKVIP ELTFDIYGEG
GERQKLQEII AKNKANNYIR LMGHKNLSSV YKDYQVYLSG STSEGFGLTL MEAIGSGLPI
IGLDVPYGNQ TFIENNLNGY LIPRETPDNP QQISTAFAQY IVALFNSKDI CKKHEYSYRI
ASRFLNDKII ENWSFFLRRL LNDYTI
