GTFB_STRGN
ID GTFB_STRGN Reviewed; 450 AA.
AC Q79T00;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 48.
DE RecName: Full=UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB {ECO:0000255|HAMAP-Rule:MF_01473};
DE AltName: Full=Glycosyltransferase stabilizing protein GtfB {ECO:0000255|HAMAP-Rule:MF_01473};
DE AltName: Full=orf4;
GN Name=gtfB {ECO:0000255|HAMAP-Rule:MF_01473, 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].
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 1-447 IN COMPLEX WITH GTFA,
RP FUNCTION, POSSIBLE REACTION MECHANISM, PATHWAY, SUBUNIT, AND MUTAGENESIS OF
RP ASP-6; ASP-14; LYS-111 AND GLU-222.
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. A
CC substrate-binding protein that is part of the accessory SecA2/SecY2
CC system specifically required to export GspB. The GtfA-GtfB complex adds
CC GlcNAc from UDP-GlcNAc to GspB, attaching the first sugar residue. Upon
CC coexpression in E.coli with GtfA glycosylates GspB constructs
CC (PubMed:15489421). Binds the GspB protein substrate; alone this subunit
CC only recognizes partially glycosylated GspB, but is constrained by GtfA
CC to also recognize unglycosylated protein. The enzyme probably modifies
CC its tertiary conformation by opening and closing its intersubunit
CC interfaces to accomodate the increasingly glycosylated substrate
CC (Probable). {ECO:0000269|PubMed:15489421, ECO:0000305|PubMed:26884191}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01473, 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: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
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:15049820, ECO:0000269|PubMed:15489421}.
CC -!- SIMILARITY: Belongs to the GtfB family. {ECO:0000305}.
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DR EMBL; AY028381; AAS86345.1; -; Genomic_DNA.
DR PDB; 5E9T; X-ray; 2.92 A; B/D=1-447.
DR PDB; 5E9U; X-ray; 3.84 A; B/D/F/H=1-446.
DR PDBsum; 5E9T; -.
DR PDBsum; 5E9U; -.
DR AlphaFoldDB; Q79T00; -.
DR SMR; Q79T00; -.
DR CAZy; GT8; Glycosyltransferase Family 8.
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; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01473; GtfB; 1.
DR InterPro; IPR014268; GtfB.
DR TIGRFAMs; TIGR02919; TIGR02919; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane.
FT CHAIN 1..450
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase stabilizing protein GtfB"
FT /id="PRO_0000414595"
FT MUTAGEN 6
FT /note="D->A: Defect in early glycosylation of GspB,
FT decreased binding of partially glycosylated GspB. Nearly
FT complete loss of glycosylation and binding to partially
FT glycosylated GspB; when associated with A-14 and A-222."
FT /evidence="ECO:0000269|PubMed:26884191"
FT MUTAGEN 14
FT /note="D->A: Mild defect in early glycosylation of GspB.
FT Nearly complete loss of glycosylation and binding to
FT partially glycosylated GspB; when associated with A-6 and
FT A-222."
FT /evidence="ECO:0000269|PubMed:26884191"
FT MUTAGEN 111
FT /note="K->C: Increased GspB glycosylation, probably forms
FT an intra-subunit disulfide bond that increases
FT tetramerization."
FT /evidence="ECO:0000269|PubMed:26884191"
FT MUTAGEN 222
FT /note="E->A: Significant defect in glycosylation of GspB in
FT vivo and in vitro, significantly decreased binding of
FT partially glycosylated GspB. Nearly complete loss of
FT glycosylation and binding to partially glycosylated GspB;
FT when associated with A-14 and A-16."
FT /evidence="ECO:0000269|PubMed:26884191"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 71..74
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 138..144
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 148..155
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 170..175
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 208..211
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 230..237
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 264..268
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 300..306
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 310..315
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 333..338
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 352..356
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 366..372
FT /evidence="ECO:0007829|PDB:5E9T"
FT STRAND 376..379
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 392..394
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 400..404
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 405..409
FT /evidence="ECO:0007829|PDB:5E9T"
FT TURN 410..412
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 415..428
FT /evidence="ECO:0007829|PDB:5E9T"
FT HELIX 434..442
FT /evidence="ECO:0007829|PDB:5E9T"
SQ SEQUENCE 450 AA; 51531 MW; B1C80A2ED34B60B3 CRC64;
MIQLFDYYNQ ETQDLHDSLL AAGYACPTIV IEANGFLPDD MISPYTYFLG DEEGVDHPLF
FNQVPVPPFW EITGDHQVAR VSDMGEERAR IHYASQARGR LVKQVDWLDK KGQLRLSERY
NKQGRCFAKT AYKSGQEAFN TTYYSTDGQE RIVENHVTGD IILTLDQEPL RIFKSRVDFI
RFFLERLDLD LDHILFNSLA YSFLVSHSLT GRAGQDILFW QEPLYDELPG NMQLILDNSQ
LRTQTIVIPD LATYEKAMSL AAADQQQKFL HLGYHYDFKR DNYLRKDALI LTHSDQIEGL
DTLVQSLPQL VFRIAALTEM SPKLLSMLSY KNVVLYQNAS LKQIEQLYLE SDIYLDINHG
GQVLQAVRKA FENNLLILGF EQTLHDRHYI AQQHIFDSSQ PAQLASILEE ALCGVEQMRS
ALQAQGRHAN DVPVSLYQET LQSLLGGQHG
