GTFB_STRPA
ID GTFB_STRPA Reviewed; 439 AA.
AC A1C3M0;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 25-MAY-2022, entry version 30.
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:16997950};
GN Name=gtfB {ECO:0000255|HAMAP-Rule:MF_01473};
GN Synonyms=gtf2 {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].
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 87-96; 129-140; 166-173; 175-183; 213-236; 254-261;
RP 276-282; 328-339 AND 420-428, FUNCTION IN GLYCOSYLATION OF FAP1, PATHWAY,
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 PROTEIN SEQUENCE OF 100-121; 131-141; 174-184; 254-261; 268-275 AND
RP 327-339, FUNCTION IN GLYCOSYLATION OF FAP1, PATHWAY, INTERACTION WITH GTFA,
RP AND DISRUPTION 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 FUNCTION AS A STABILIZING PROTEIN, PATHWAY, SUBCELLULAR LOCATION,
RP DISRUPTION PHENOTYPE, AND MUTAGENESIS OF 35-GLY--PRO-38; 57-PRO--PHE-60;
RP 61-ASN--ASP-64; 148-GLN--LEU-151; 159-ASP--LEU-162 AND 315-THR--SER-318.
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 the polymorphic O-glycosylation of the serine-
CC rich repeat protein Fap1. A stabilizing protein that is part of the
CC accessory SecA2/SecY2 system specifically required to export Fap1, a
CC serine-rich fimbrial adhesin encoded upstream in the same operon. The
CC GtfA-GtfB (Gtf1-Gtf2 in this bacteria) complex adds GlcNAc from UDP-
CC GlcNAc to Fap1, attaching the first sugar residue. Cannot use not UDP-
CC Glc as substrate. Stabilizes the glycosylation activity of GtfA,
CC causing it to partially localize to the cellular membrane where it is
CC more protease resistant. {ECO:0000269|PubMed:18083807,
CC ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:18083807,
CC ECO:0000269|PubMed:20971868, ECO:0000269|PubMed:21862581}.
CC -!- SUBUNIT: Interacts with glycosyltransferase GtfA (Gtf2); probably forms
CC a heterotetramer with 2 subunits each of GtfA and GtfB. Part of the
CC accessory SecA2/SecY2 protein translocation apparatus.
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:18083807,
CC ECO:0000269|PubMed:20971868}.
CC -!- INTERACTION:
CC A1C3M0; A1C3L9: gtfA; NbExp=6; IntAct=EBI-6401543, EBI-6401548;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21862581};
CC Peripheral membrane protein {ECO:0000305|PubMed:21862581}.
CC -!- DISRUPTION PHENOTYPE: No glycosylation of serine-rich fimbrial adhesin
CC Fap1. The unglycosylated version of Fap1 accumulates which is larger
CC than the wild-type protein. In a deletion mutant, GtfA (Gtf1) is less
CC stable in vivo, no longer associates with the cell membrane and has an
CC increased protease susceptibility. Biofilm formation decreases. In a
CC double gftA/gtfB (gtf1/gtf2) mutant, there is no further affect on
CC glycosylation but biofilm formation is further decreased.
CC {ECO:0000269|PubMed:18083807, ECO:0000269|PubMed:21862581}.
CC -!- SIMILARITY: Belongs to the GtfB family. {ECO:0000305}.
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DR EMBL; DQ990875; ABL74005.1; -; Genomic_DNA.
DR RefSeq; WP_014713988.1; NZ_JYPA01000019.1.
DR AlphaFoldDB; A1C3M0; -.
DR SMR; A1C3M0; -.
DR IntAct; A1C3M0; 1.
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:CACAO.
DR GO; GO:0006486; P:protein glycosylation; IEA:UniProtKB-UniPathway.
DR GO; GO:0031647; P:regulation of protein stability; IDA: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; Direct protein sequencing; Membrane.
FT CHAIN 1..439
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase stabilizing protein GtfB"
FT /id="PRO_0000418642"
FT MUTAGEN 35..38
FT /note="Missing: Loss of Fap1 glycosylation, decreased
FT association of GtfA with the cell membrane. Reduced GtfB
FT levels."
FT /evidence="ECO:0000269|PubMed:21862581"
FT MUTAGEN 57..60
FT /note="Missing: Loss of Fap1 glycosylation, reduced GtfA-
FT GtfB interaction, about 18% Fap1 glycosylation, loss of
FT GtfA and Fap1 stability in vivo, decreased association of
FT GtfA with the cell membrane."
FT /evidence="ECO:0000269|PubMed:21862581"
FT MUTAGEN 61..64
FT /note="Missing: Loss of Fap1 glycosylation, reduced GtfA-
FT GtfB interaction, about 20% Fap1 glycosylation, decreased
FT association of GtfA with the cell membrane."
FT /evidence="ECO:0000269|PubMed:21862581"
FT MUTAGEN 148..151
FT /note="Missing: Loss of Fap1 glycosylation, decreased
FT association of GtfA with the cell membrane. Reduced GtfB
FT levels."
FT /evidence="ECO:0000269|PubMed:21862581"
FT MUTAGEN 159..162
FT /note="Missing: Loss of Fap1 glycosylation, decreased
FT association of GtfA with the cell membrane. Reduced GtfB
FT levels."
FT /evidence="ECO:0000269|PubMed:21862581"
FT MUTAGEN 315..318
FT /note="Missing: Wild-type Fap1 glycosylation, no reduction
FT in GtfA-GtfB interaction, about 69% Fap1 glycosylation."
FT /evidence="ECO:0000269|PubMed:21862581"
SQ SEQUENCE 439 AA; 51363 MW; 25FFBBF4D820C0FD CRC64;
MIRLFEWLTQ ESLDLHYSLE ESGIHGTSIV LNDDGFLPEG IISPYTFFCE VEMDGSPLYF
NQLEVPYLWQ ITGTNIEGEI WNRSSKRGVI HYHEPKYLRF VQSVDWLYPD GSIYMTDHYN
KYGWAFARTY FFSDQQVSHK KYYTKSGQEV LSENILTGDI LLNWKGKVYH FTKKVDFFLF
YFKKSGLDLS SIWYNSLGMP FLISYYLGGE GRDILFWQEN LADQLPGNMQ IIFSGRTSRT
KKVIVQDRSV YKKLLHLVEE KNKEMISFLN IIYPKLRENY SRKEILIVTN SDQIEGIETL
TDNLSAYTFH IGALTSMSDK LQNIGQKENV LLYPNMSPKT MLDLLEQCDI YLDINHGNEV
LSIVRLAFER SLLILAYDNT VHSPIFHHES GIFNHSKPQT LSDWLLNLDD YSQTVSCWRS
DLFPMTYRDY KQVLVSNVD
