ID   GTFB_LIMR5              Reviewed;         441 AA.
AC   A0A0S4NND9; F8KEI4;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   17-FEB-2016, sequence version 1.
DT   25-MAY-2022, entry version 25.
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};
GN   Name=gtfB {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000303|PubMed:30371779};
GN   ORFNames=LRATCC53608_1097;
OS   Limosilactobacillus reuteri (strain ATCC 53608) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=927703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53608;
RX   PubMed=21622738; DOI=10.1128/jb.05282-11;
RA   Heavens D., Tailford L.E., Crossman L., Jeffers F., Mackenzie D.A.,
RA   Caccamo M., Juge N.;
RT   "Genome sequence of the vertebrate gut symbiont Lactobacillus reuteri ATCC
RT   53608.";
RL   J. Bacteriol. 193:4015-4016(2011).
RN   [2]
RP   FUNCTION, AND PATHWAY.
RC   STRAIN=ATCC 53608;
RX   PubMed=30371779; DOI=10.1093/glycob/cwy100;
RA   Latousakis D., Nepravishta R., Rejzek M., Wegmann U., Le Gall G.,
RA   Kavanaugh D., Colquhoun I.J., Frese S., MacKenzie D.A., Walter J.,
RA   Angulo J., Field R.A., Juge N.;
RT   "Serine-rich repeat protein adhesins from Lactobacillus reuteri display
RT   strain specific glycosylation profiles.";
RL   Glycobiology 29:45-58(2019).
CC   -!- FUNCTION: Required for polymorphic O-glycosylation of the serine-rich
CC       repeat protein (SRRP) in this bacteria. A stabilizing protein that is
CC       part of the accessory SecA2/SecY2 system specifically required to
CC       export serine-rich repeat cell wall proteins encoded in the same
CC       operon. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to the
CC       substrate protein, attaching the first sugar residue. Stabilizes the
CC       glycosylation activity of GtfA. Has no N-acetylglucosaminyl transferase
CC       activity on its own. {ECO:0000255|HAMAP-Rule:MF_01473}.
CC   -!- PATHWAY: Protein modification; protein glycosylation.
CC       {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:30371779}.
CC   -!- SUBUNIT: Forms a heterotetramer with 2 subunits each of GtfA and GtfB.
CC       Part of the accessory SecA2/SecY2 protein translocation apparatus.
CC       {ECO:0000255|HAMAP-Rule:MF_01473}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
CC   -!- SIMILARITY: Belongs to the GtfB family. {ECO:0000255|HAMAP-
CC       Rule:MF_01473}.
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DR   EMBL; FR854365; CCC03849.1; -; Genomic_DNA.
DR   RefSeq; WP_003675575.1; NZ_LN906634.1.
DR   AlphaFoldDB; A0A0S4NND9; -.
DR   SMR; A0A0S4NND9; -.
DR   HOGENOM; CLU_050378_0_0_9; -.
DR   UniPathway; UPA00378; -.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0017122; C:protein N-acetylglucosaminyltransferase complex; IEA:UniProtKB-UniRule.
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   3: Inferred from homology;
KW   Cell membrane; Membrane.
FT   CHAIN           1..441
FT                   /note="UDP-N-acetylglucosamine--peptide N-
FT                   acetylglucosaminyltransferase stabilizing protein GtfB"
FT                   /id="PRO_0000447249"
SQ   SEQUENCE   441 AA;  51614 MW;  F78415DDB48BC5B9 CRC64;
     MLNLFDNFDQ ASFDFLRSQR TAQIKIPTVV INDDGFLPPE VESPIKYWGN YNVNKKPLYF
     DHLSLPRYWR ILSTAAQGHI YDLDKKRADI IYQATDNTRQ VKEVRWLNNN GKVSWIDHYN
     RYGYRFAQTY YRNEQPAWRK YYDKKNRVFL EWNLIAGDFF LDVDGGYHFP SLIELVKYYL
     QTRHFKLDHI FYNTLNQGLS VSLNLPADGS DTLFWHEPLS GDELPGNMKF LMENSTRTKH
     IIFQRYTDWQ RIGANLKNNH VDFGFLGTIY PHPRANQLRP QALILTNSDE IVELSTLIKN
     LPNIKFHIAA VTEMSGKLLA YQQYENVELY PNVSSARVKQ LIADCDIYLD INRQNEILDA
     VRGAFEQNML IVGFDETLHE PQFVTPQNMF KVNEAQKMSK HIMAALLKPA LMKELIDTQR
     QLASEVSVQD YQRMIGALQS E