GTFA_STRGN
ID GTFA_STRGN Reviewed; 506 AA.
AC Q9AET5;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 68.
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:26884191};
DE AltName: Full=Glycosyltransferase GtfA {ECO:0000255|HAMAP-Rule:MF_01472};
DE AltName: Full=O-glycosyltransferase {ECO:0000303|PubMed:26884191};
GN Name=gtfA {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000303|PubMed:26884191};
OS Streptococcus gordonii.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1302;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=12010500; DOI=10.1046/j.1365-2958.2002.02949.x;
RA Bensing B.A., Sullam P.M.;
RT "An accessory sec locus of Streptococcus gordonii is required for export of
RT the surface protein GspB and for normal levels of binding to human
RT platelets.";
RL Mol. Microbiol. 44:1081-1094(2002).
RN [2]
RP DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=15049820; DOI=10.1111/j.1365-2958.2004.03978.x;
RA Takamatsu D., Bensing B.A., Sullam P.M.;
RT "Genes in the accessory sec locus of Streptococcus gordonii have three
RT functionally distinct effects on the expression of the platelet-binding
RT protein GspB.";
RL Mol. Microbiol. 52:189-203(2004).
RN [3]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=M99;
RX PubMed=15489421; DOI=10.1128/jb.186.21.7100-7111.2004;
RA Takamatsu D., Bensing B.A., Sullam P.M.;
RT "Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii
RT mediate the intracellular glycosylation of the platelet-binding protein
RT GspB.";
RL J. Bacteriol. 186:7100-7111(2004).
RN [4] {ECO:0007744|PDB:5E9T, ECO:0007744|PDB:5E9U}
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 2-503 IN COMPLEX WITH GTFB;
RP N-ACETYL-D-GLUCOSAMINE AND UDP, FUNCTION, SUBSTRATE SPECIFICITY, POSSIBLE
RP REACTION MECHANISM, PATHWAY, SUBUNIT, AND DOMAIN.
RC STRAIN=M99;
RX PubMed=26884191; DOI=10.1073/pnas.1600494113;
RA Chen Y., Seepersaud R., Bensing B.A., Sullam P.M., Rapoport T.A.;
RT "Mechanism of a cytosolic O-glycosyltransferase essential for the synthesis
RT of a bacterial adhesion protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 113:E1190-E1199(2016).
CC -!- FUNCTION: Required for polymorphic O-glycosylation of GspB, a serine-
CC rich repeat cell wall protein encoded upstream in the same operon.
CC Catalyzes the first step in glycosylation by transferring N-
CC acetylglucosamine from UDP-GlcNAc to serine residues in GspB. Part of
CC the accessory SecA2/SecY2 system specifically required to export GspB.
CC Upon coexpression in E.coli with GtfB glycosylates GspB constructs.
CC Glycosylation probably occurs intracellularly (PubMed:15489421).
CC Requires GtfB for glycosylation activity, it has no activity alone.
CC Does not use UDP-glucose as substrate. Has a fast, probably processive
CC glycosylation phase followed by a slower, non-processive phase. The
CC enzyme probably modifies its tertiary conformation by opening and
CC closing its intersubunit interfaces to accomodate the increasingly
CC glycosylated substrate; protein substrate recognition is provided by
CC GtfB (PubMed:26884191). {ECO:0000269|PubMed:15489421,
CC ECO:0000269|PubMed:26884191}.
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;
CC Evidence={ECO:0000250|UniProtKB:A0A0H2URG7,
CC ECO:0000250|UniProtKB:A0A0S4NM89, ECO:0000255|HAMAP-Rule:MF_01472,
CC ECO:0000305|PubMed:26884191};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01472, ECO:0000269|PubMed:15489421,
CC ECO:0000269|PubMed:26884191}.
CC -!- SUBUNIT: Forms a heterotetramer with 2 subunits each of GtfA and GtfB
CC (PubMed:26884191). Part of the accessory SecA2/SecY2 protein
CC translocation apparatus required to export cell wall protein GspB
CC (Probable). {ECO:0000269|PubMed:26884191, ECO:0000305|PubMed:15489421,
CC ECO:0000305|PubMed:26884191}.
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 -!- DOMAIN: Has 2 Rossmann-like domains, called R-fold-1 and R-fold-2. R-
CC fold-1 is interrupted by an extended beta-sheet domain that loops out
CC of the structure. UDP and N-acetyl-D-glucosamine bind between the
CC Rossman-like folds, which move closer together upon binding.
CC {ECO:0000269|PubMed:26884191}.
CC -!- DISRUPTION PHENOTYPE: Loss of export of cell wall protein GspB;
CC transcription should not be affected. Non-glycosylated GspB may form
CC aggregates. {ECO:0000269|PubMed:12010500, ECO:0000269|PubMed:15049820,
CC ECO:0000269|PubMed:15489421}.
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; AY028381; AAK17002.2; -; Genomic_DNA.
DR PDB; 5E9T; X-ray; 2.92 A; A/C=2-503.
DR PDB; 5E9U; X-ray; 3.84 A; A/C/E/G=2-503.
DR PDBsum; 5E9T; -.
DR PDBsum; 5E9U; -.
DR AlphaFoldDB; Q9AET5; -.
DR SMR; Q9AET5; -.
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:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0006493; P:protein O-linked glycosylation; IDA:UniProtKB.
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 3D-structure; 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_0000414593"
FT REGION 1..78
FT /note="N-terminus R-fold-1"
FT /evidence="ECO:0000305|PubMed:26884191"
FT REGION 79..195
FT /note="Extended beta-sheet domain"
FT /evidence="ECO:0000305|PubMed:26884191"
FT REGION 196..306
FT /note="C-terminus R-fold-1"
FT /evidence="ECO:0000305|PubMed:26884191"
FT REGION 307..506
FT /note="R-fold-2"
FT /evidence="ECO:0000305|PubMed:26884191"
FT BINDING 16..19
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472,
FT ECO:0007744|PDB:5E9U"
FT BINDING 242
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01472,
FT ECO:0007744|PDB:5E9U"
FT BINDING 328
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0007744|PDB:5E9U"
FT BINDING 357
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0007744|PDB:5E9U"
FT BINDING 383..385
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0007744|PDB:5E9U"
FT BINDING 405..407
FT /ligand="N-acetyl-D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:506227"
FT /evidence="ECO:0007744|PDB:5E9U"
FT BINDING 409
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0007744|PDB:5E9U"
FT STRAND 3..7
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 17..30
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 48..55
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 88..90
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 107..110
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 111..119
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 124..132
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 135..155
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 158..167
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 171..180
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 183..188
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 197..208
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 222..224
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 225..232
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 235..241
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 246..248
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 260..267
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 269..271
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 273..278
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 280..293
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 299..302
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 322..326
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 331..333
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 336..348
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 353..357
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 364..372
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 379..381
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 388..390
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 394..398
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 404..406
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 408..415
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 428..432
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 435..437
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 438..442
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 451..462
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 471..473
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 482..484
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 486..500
FT /evidence="ECO:0007829|PDB:5E9T"
SQ SEQUENCE 506 AA; 58313 MW; 2C117FA5DB155C93 CRC64;
MTVYNINLGI GWASSGVEYA QAYRAQILRR IQQPAKFIFM DMILADNIQH LTENIGFLDE
EIIWLYNYFT DIKIAPTTVT LDQVLAQVAG QPERSEKEGK IVRYFYPQDD QFITCYLRQE
DQDSVEHVEY VSRGRLIRKD YFSYVRYASE YFAPHNDAAT LYQRRFYHED GSVAYDMLIE
DGQEKLYRFP DRIFYSKAEL VRYFLQCLQL QADDVVILDR ETGIGQVVFE ESQKAKLGVV
VHAEHFSENA SSDDYILWNN FYDYQFTNAD KVDFFIVATE AQKRILEQQF QHYSDKQPQI
ATIPVGSLDQ LTYPKEPRKP YSMITASRLA TEKHIDWLVA ATVQAHAQLP ELTLDIYGKG
SEEDKLRRRI EEAGAQDYIR LKGHADLSQI YAGYELYLTA STSEGFGLTL MEAVGSGLPL
IGFDVRYGNQ TFIDDGKNGY LLPVSSNHVE DQIIAAFVEK IIALFSQGRQ QEMSQHSYQV
AENYLTSRVE AAWTQLLKEV RDDSAL
