GTFB_STRPN
ID GTFB_STRPN Reviewed; 445 AA.
AC A0A0H2UR90;
DT 08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-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, ECO:0000303|PubMed:24936067};
GN Name=gtfB {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000303|PubMed:24936067};
GN OrderedLocusNames=SP_1757;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
RN [2]
RP DISCUSSION OF SEQUENCE.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=16861665; DOI=10.1128/iai.00316-06;
RA Obert C., Sublett J., Kaushal D., Hinojosa E., Barton T., Tuomanen E.I.,
RA Orihuela C.J.;
RT "Identification of a candidate Streptococcus pneumoniae core genome and
RT regions of diversity correlated with invasive pneumococcal disease.";
RL Infect. Immun. 74:4766-4777(2006).
RN [3]
RP FUNCTION, PATHWAY, SUBUNIT, AND DOMAIN.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=24936067; DOI=10.1074/jbc.m114.581934;
RA Shi W.W., Jiang Y.L., Zhu F., Yang Y.H., Shao Q.Y., Yang H.B., Ren Y.M.,
RA Wu H., Chen Y., Zhou C.Z.;
RT "Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc)
RT transferase, GtfA, reveals insights into the glycosylation of pneumococcal
RT serine-rich repeat adhesins.";
RL J. Biol. Chem. 289:20898-20907(2014).
RN [4]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=28246170; DOI=10.1074/jbc.m116.770446;
RA Jiang Y.L., Jin H., Yang H.B., Zhao R.L., Wang S., Chen Y., Zhou C.Z.;
RT "Defining the enzymatic pathway for polymorphic O-glycosylation of the
RT pneumococcal serine-rich repeat protein PsrP.";
RL J. Biol. Chem. 292:6213-6224(2017).
CC -!- FUNCTION: Required for the polymorphic O-glycosylation of the serine-
CC rich repeat protein PsrP. A stabilizing protein that is part of the
CC accessory SecA2/SecY2 system specifically required to export serine-
CC rich repeat cell wall proteins encoded upstream in the same operon. The
CC GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP, attaching the
CC first sugar residue. Stabilizes the glycosylation activity of GtfA (By
CC similarity) (PubMed:24936067, PubMed:28246170). Has no N-
CC acetylglucosaminyl transferase activity on its own (PubMed:24936067).
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:24936067,
CC ECO:0000269|PubMed:28246170}.
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000255|HAMAP-Rule:MF_01473, ECO:0000269|PubMed:24936067,
CC ECO:0000269|PubMed:28246170}.
CC -!- SUBUNIT: Interacts with glycosyltransferase GtfA; probably forms a
CC 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:24936067}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
CC -!- DOMAIN: The N-terminus of the protein, including the
CC glycosyltransferase 1 domain (residues 1-171), is required but not
CC sufficient for full formation of the stable GtfA-GtfB complex; the
CC complex of GtfA with truncated GtfB has intermediate N-
CC acetylglucosaminyl transferase activity. {ECO:0000269|PubMed:24936067}.
CC -!- MISCELLANEOUS: Encoded in RD10, a pathogenicity island with an atypical
CC GC content that is associated with invasive pneumococcal disease.
CC Pathogenicity islands account for greater than half the genomic
CC diversity observed between isolates (PubMed:11463916, PubMed:16861665).
CC The main function of this island seems to be correct synthesis and
CC export of pneumococcal serine-rich repeat protein PsrP (Probable).
CC {ECO:0000303|PubMed:11463916, ECO:0000303|PubMed:16861665,
CC ECO:0000305}.
CC -!- SIMILARITY: Belongs to the GtfB family. {ECO:0000255|HAMAP-
CC Rule:MF_01473}.
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DR EMBL; AE005672; AAK75832.1; -; Genomic_DNA.
DR RefSeq; WP_000571767.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; A0A0H2UR90; -.
DR SMR; A0A0H2UR90; -.
DR STRING; 170187.SP_1757; -.
DR EnsemblBacteria; AAK75832; AAK75832; SP_1757.
DR KEGG; spn:SP_1757; -.
DR eggNOG; COG0438; Bacteria.
DR OMA; QNASPQK; -.
DR BioCyc; SPNE170187:G1FZB-1782-MON; -.
DR UniPathway; UPA00378; -.
DR Proteomes; UP000000585; Chromosome.
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 Cell membrane; Membrane.
FT CHAIN 1..445
FT /note="UDP-N-acetylglucosamine--peptide N-
FT acetylglucosaminyltransferase stabilizing protein GtfB"
FT /id="PRO_0000447203"
FT REGION 55..171
FT /note="Glycosyltransferase 1"
FT /evidence="ECO:0000269|PubMed:24936067"
SQ SEQUENCE 445 AA; 50673 MW; 8A2E2DD880CFD53C CRC64;
MIELYDSYSQ ESRDLHESLG ATGLSQLGVV IDADGFLPDG LLSPFTYYLG YEDGKPLYFN
QVPVSDFWEI LGDNQSACIE DVTQERAVIH YADGMQARLV KQVDWKDLEG RVRQVDHYNR
FGACFATTTY SADSEPIMTV YQDVNGQQVL LENHVTGDIL LTLPGQSMRY FANKVEFITF
FLQDLEIDTS QLIFNTLATP FLVSFHHPDK SGSDVLVWQE PLYDAIPGNM QLILESDNVR
TKKIIIPNKA TYERALELTD EKYHDQFVHL GYHYQFKRDN FLRRDALILT NSDQIEQVEA
IAGALPDVTF RIAAVTEMSS KLLDMLCYPN VALYQNASPQ KIQELYQLSD IYLDINHSNE
LLQAVRQAFE HNLLILGFNQ TVHNRLYIAP DHLFESSEVA ALVETIKLAL SDVDQMRQAL
GKQGQHANYV DLVRYQETMQ TVLGG
