ProGP453

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ProGP ID ProGP453
Validation Status Characterized
Organism Information
Organism NameStreptococcus pneumoniae
Domain Bacteria
Classification Family: Bacillaceae
Order: Bacillales
Class: Bacilli (or Firmibacteria)
Division or phylum: "Firmicutes"
Taxonomic ID (NCBI) 1313
Genome Sequence(s)
GenBank CQYP01000015.1
EMBL CQYP01000015.1
Gene Information
Gene NamepsrP
GenBank Gene Sequence CQYP01000015.1
Protein Information
Protein NamePsrP (Adhesin)
UniProtKB/SwissProt ID A0A0U0B015
NCBI RefSeq COC00526.1
EMBL-CDSCOC00526.1
UniProtKB Sequence >tr|A0A0U0B015|A0A0U0B015_STREE Large surface exposed glycoprotein PsrP OS=Streptococcus pneumoniae GN=psrP PE=4 SV=1 MRGGVDTTQVMTETVEDKVSHSITGLDILKGIAAVGAVISGTVATQTKVFTNESAVLEKT VEKTDALATNGTVVLGTISTSNSASSTSLSASESASTSASESASTSASTSASTSASESAS TSASISISASSTVVGSQTAAATEATAKKVEEDRKKLASDYAASVTNVNLQSYANRRKRSV DSIEQLLASIKAAVFSGNTIVNGAPAINASLNIAKSETKIYTGTGRDSFYNIPIYYKLTV TNDGSELTFTYTVTYVNPTTRALENLSRMSYGYSIYNTGTSTQTMLTLGSGLGTPSGVTN SITNKNGAQVQRYNISTMTTKGSGYTWGNGAQMNGWQAKKGYGLTSSWTVPIIGTDTSFT FTPYAAKTDRIGINYFKGRGKVVESSTTSQSLSQSKSLSVSASQSASASASTSASASAST SASASASTSASASASTSASASASISASESASTSASESASTSASASASISASESASTSASA SASTSASESASTSASESASTSASASASTSASESASTSASVSASTSANRSGQSNRFLTMF
Sequence length 539 AA
Function Pneumococcal serine-rich repeat protein involved in infection and pathogenesis.
Glycosylation Status
Glycosylation Type O- (Ser) linked
Experimentally Validated Glycosite(s) in Full Length ProteinS2, S4, S5, S7, S9, S11, S23, S29, S37, S39, S47, S49 and S50 in the first SRR of PsrP.
Glycosite(s) Annotated Protein Sequence >tr|A0A0U0B015|A0A0U0B015_STREE Large surface exposed glycoprotein PsrP OS=Streptococcus pneumoniae GN=psrP PE=4 SV=1 MRGGVDTTQVMTETVEDKVSHSITGLDILKGIAAVGAVISGTVATQTKVFTNESAVLEKT VEKTDALATNGTVVLGTISTSNS*(2)AS*(4)S*(5)TS*(7)LS*(9)AS*(11)ESASTSASESAS*(23)TSASTS*(29)ASTSASES*(37)AS*(39) TSASISIS*(47)AS*(49)S*(50)TVVGSQTAAATEATAKKVEEDRKKLASDYAASVTNVNLQSYANRRKRSV DSIEQLLASIKAAVFSGNTIVNGAPAINASLNIAKSETKIYTGTGRDSFYNIPIYYKLTV TNDGSELTFTYTVTYVNPTTRALENLSRMSYGYSIYNTGTSTQTMLTLGSGLGTPSGVTN SITNKNGAQVQRYNISTMTTKGSGYTWGNGAQMNGWQAKKGYGLTSSWTVPIIGTDTSFT FTPYAAKTDRIGINYFKGRGKVVESSTTSQSLSQSKSLSVSASQSASASASTSASASAST SASASASTSASASASTSASASASISASESASTSASESASTSASASASISASESASTSASA SASTSASESASTSASESASTSASASASTSASESASTSASVSASTSANRSGQSNRFLTMF
Glycosite Sequence Logo
Technique(s) used for Glycosylation DetectionAltered mobility on blots after in vitro O-GlcNAcylation
Technique(s) used for Glycosylated Residue(s) Detection LC-MS analysis after in vitro O-GlcNAcylation
Protein Glycosylation- Implication Glycosylation by O-GlcNAc is required for pathogenicity of S. pneumoniae.
Glycan Information
Glycan Annotation GlcNAc
Protein Glycosylation linked (PGL) gene(s)
OST ProGT IDProGT77,ProGT78
Additional CommentThe study also suggests that fusion with the novel add-on domain might be a universal mechanism for diverse OGTs. A peptide of proper length is necessary for the in vitro O-GlcNAcylation of SRR1. Using in vivo E. coli glycosylation system, co-expression of GtfA-GtfB was observed to O-GlcNAcylate recombinant PsrP, which was also found to bind GtfA. With site-directed mutagenesis, Glu-332 of GtfA was found to be catalytically essential. While the mutation of highly conserved Glu-244 and catalytic Glu-332 to alanine completely abolished the O-GlcNAcylation activity, mutation of Ser-403 significantly diminished the activity.
Literature
Year of Identification2014
Year of Identification Month Wise2014.1.1
Year of Validation 2014
ReferenceShi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ. (2014) Structure of a novel O-linked N-acetyl-D-glucosamine (O-GlcNAc) transferase, GtfA, reveals insights into the glycosylation of pneumococcal serine-rich repeat adhesins. J Biol Chem., 289(30):20898-907. [PMID: 24936067]
AuthorShi WW, Jiang YL, Zhu F, Yang YH, Shao QY, Yang HB, Ren YM, Wu H, Chen Y, Zhou CZ.
Research GroupDepartments of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama
Corresponding Author Zhou CZ.
ContactDepartments of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama