GTFA_STRPA
ID GTFA_STRPA Reviewed; 504 AA.
AC A1C3L9;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 42.
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, ECO:0000269|PubMed:20971868};
DE AltName: Full=Glycosyltransferase Gtf1 {ECO:0000303|PubMed:16997950};
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:16997950};
OS Streptococcus parasanguinis.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1318;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=FW213;
RX PubMed=16997950; DOI=10.1128/jb.00836-06;
RA Wu H., Bu S., Newell P., Chen Q., Fives-Taylor P.;
RT "Two gene determinants are differentially involved in the biogenesis of
RT Fap1 precursors in Streptococcus parasanguis.";
RL J. Bacteriol. 189:1390-1398(2007).
RN [2]
RP PROTEIN SEQUENCE OF 82-94; 149-166; 186-193; 214-250; 273-282; 285-313;
RP 350-365 AND 374-383, FUNCTION AS A GLYCOSYLTRANSFERASE, CATALYTIC ACTIVITY,
RP AND SUBUNIT.
RC STRAIN=FW213;
RX PubMed=20971868; DOI=10.1128/aem.01434-10;
RA Wu R., Zhou M., Wu H.;
RT "Purification and characterization of an active N-
RT acetylglucosaminyltransferase enzyme complex from Streptococci.";
RL Appl. Environ. Microbiol. 76:7966-7971(2010).
RN [3]
RP FUNCTION IN GLYCOSYLATION OF FAP1, INTERACTION WITH GTFB, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=FW213;
RX PubMed=18083807; DOI=10.1128/jb.01078-07;
RA Bu S., Li Y., Zhou M., Azadin P., Zeng M., Fives-Taylor P., Wu H.;
RT "Interaction between two putative glycosyltransferases is required for
RT glycosylation of a serine-rich streptococcal adhesin.";
RL J. Bacteriol. 190:1256-1266(2008).
RN [4]
RP STABILIZATION BY GTFB (GTF2), INTERACTION WITH GTFB, SUBCELLULAR LOCATION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=FW213;
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 serine-rich
CC repeat protein Fap1. Catalyzes the first step in glycosylation by
CC transferring N-acetylglucosamine from UDP-GlcNAc to serine residues in
CC Fap1. Part of the accessory SecA2/SecY2 system specifically required to
CC export Fap1, a serine-rich fimbrial adhesin encoded upstream in the
CC same operon. The GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds
CC GlcNAc from UDP-GlcNAc to Fap1, attaching the first sugar residue.
CC Cannot use not UDP-Glc as substrate. This subunit has very low
CC glycosyltransferase activity; the GtfB stabilizing protein enhances
CC membrane association, protease resistance and glycosyltransferase
CC activity. {ECO:0000269|PubMed:16997950, ECO:0000269|PubMed:18083807,
CC ECO:0000269|PubMed:20971868}.
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}.
CC -!- SUBUNIT: Interacts with stabilizing protein GtfB (Gtf1), probably via
CC the N-terminus of this protein; probably forms a heterotetramer with 2
CC subunits each of GtfA and GtfB. Part of the accessory SecA2/SecY2
CC protein translocation apparatus. {ECO:0000269|PubMed:18083807,
CC ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}.
CC -!- INTERACTION:
CC A1C3L9; A1C3M0: gtfB; NbExp=6; IntAct=EBI-6401548, EBI-6401543;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01472,
CC ECO:0000269|PubMed:21862581}. Cell membrane {ECO:0000255|HAMAP-
CC Rule:MF_01472, ECO:0000269|PubMed:21862581}; Peripheral membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000305|PubMed:21862581}.
CC Note=Cell membrane association requires GtfB (Gtf2), protein is more
CC active and protected from trypsin (PubMed:21862581).
CC {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:21862581}.
CC -!- DISRUPTION PHENOTYPE: No glycosylation of serine-rich fimbrial adhesin
CC Fap1, an unglycosylated version of Fap1 accumulates that is larger than
CC the wild-type protein. No further defect in a double gtfA/gtfB
CC disruption mutant, but biofilm formation is further decreased than in a
CC gtfB deletion. {ECO:0000269|PubMed:16997950,
CC ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:21862581}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000255|HAMAP-Rule:MF_01472,
CC ECO:0000305}.
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DR EMBL; DQ990875; ABL74004.1; -; Genomic_DNA.
DR RefSeq; WP_014713989.1; NZ_JYPA01000019.1.
DR AlphaFoldDB; A1C3L9; -.
DR SMR; A1C3L9; -.
DR IntAct; A1C3L9; 1.
DR CAZy; GT4; Glycosyltransferase Family 4.
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:CACAO.
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; Direct protein sequencing; Glycosyltransferase;
KW Membrane; Nucleotide-binding; Transferase.
FT CHAIN 1..504
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase GtfA subunit"
FT /id="PRO_0000414885"
FT BINDING 16..19
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 243
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 385..386
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
FT BINDING 405..408
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472"
SQ SEQUENCE 504 AA; 58239 MW; B0DDBA570024ED0E CRC64;
MTIYNINLGI GWASSGVEYA QAYRAQILRS LGMPAKFIFT NMFQSENLEH FTKNIGFEDN
EIIWLYGYFT DVKISGTTYK KDDLEATFSQ CPTKKEASSD RKLIRYYFEN QELYINASLY
GENQEYVQRV EYVVKGKLIR KDYYSYTKVF SEFYSPGENG VQLCNRSFYN EDGSIAYEEI
LSNEKSTFVF SNKICYGLEE LLEFMLEDLS LTKSDLILLD RATGIGQVVF ENIGAAKLAV
VIHAEHFNEK NTDEHNILWN NYYEYQFTNA DKVNAFITST ERQKILLEEQ FTQYTSLHPK
IVAIPVGSLD QLKFPEQSRK SFSMMTGSRL AIEKHIDWLI EGVALAQKRL PELTFDIYGE
GGERRKLTEL LTKLHAGEFI ELKGHKQLDE IYQNYELYLT ASTSEGFGLT LMEAVGSGLP
IIGFDVPYGN QTFVCSGENG LLIERPKGDD RSRIVQAFAD SIYEYFTKFK MADAQQYSYN
IAENYKHEKL VERWKDFIEE MLND
