ProGP449 (PsrP (Adhesin))

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ProGP ID ProGP449 (PsrP (Adhesin))
Validation Status Characterized
Organism Information
Organism NameStreptococcus pneumoniae
Domain Bacteria
Classification Phylum : Firmicutes
Class : Bacilli
Orders : Lactobacillales
Family : Streptococcaceae
Genus : Streptococcus
Species : pneumoniae
Taxonomic ID (NCBI) 1313
Genome Information
GenBank CQYP01000015.1
EMBL CQYP01000015.1
Gene Information
Gene NamepsrP
NCBI Gene ID CQYP01000015.1
GenBank Gene Sequence CQYP01000015.1
Protein Information
Protein NamePsrP (Adhesin)
UniProtKB/SwissProt ID UPI0005DDCA43
NCBI RefSeq COC00526.1
EMBL-CDSCOC00526.1
UniProtKB Sequence >UPI0005DDCA43 status=active 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
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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 IDProGT75 ProGT76
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, W.W., Jiang, Y.L., Zhu, F., Yang, Y.H., Shao, Q.Y., Yang, H.B., Ren, Y.M., Wu, H., Chen, Y. and Zhou, C.Z., 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. Journal of Biological Chemistry, 289(30), pp.20898-20907.
Corresponding Author Hui Wu
Yuxing Chen
Cong-Zhao Zhou
ContactDepartment of Pediatric Dentistry and Microbiology, University of Alabama at Birmingham, Schools of Dentistry and Medicine, Birmingham, Alabama 35294
Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, China