Q939N5 · GSPB_STRGN

  • Protein
    Platelet binding protein GspB
  • Gene
    gspB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA (PubMed:21765814).
Plays a positive role in biofilm formation, possibly by self-association via the basic region (BR) (PubMed:20714350).

Miscellaneous

S.gordonii, a commensal oral cavity bacteria, is among the bacteria most frequently identified as being the primary etiological agents of subacute infective endocarditis (found in 13% of cases).

Features

Showing features for site.

130722004006008001,0001,2001,4001,6001,8002,0002,2002,4002,6002,8003,000
TypeIDPosition(s)Description
Site443Important for interaction with host glycoprotein and virulence
Site484Important for interaction with host glycoprotein and virulence
Site485Important for interaction with host glycoprotein and virulence

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentextracellular region
Biological Processcell adhesion

Keywords

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Platelet binding protein GspB
  • Alternative names
    • Adhesin GspB
    • Serine-rich adhesin for platelets
    • Serine-rich repeat protein GspB

Gene names

    • Name
      gspB

Organism names

  • Taxonomic identifier
  • Strain
    • M99
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus

Accessions

  • Primary accession
    Q939N5

Subcellular Location

Secreted, cell wall
; Peptidoglycan-anchor
Note: Exported by the accessory SecA2/SecY2 protein translocation apparatus.

Keywords

Phenotypes & Variants

Disruption phenotype

Loss of adherence to human platelet cells (PubMed:12010500).
Decrease in early biofilm formation (PubMed:20714350).

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis443Strongly reduced interaction with GP1BA carbohydrate chains.
Mutagenesis484Strongly reduced interaction with GP1BA carbohydrate chains. Strongly reduced platelet binding.
Mutagenesis485Strongly reduced interaction with GP1BA carbohydrate chains.

PTM/Processing

Features

Showing features for signal, chain, modified residue, propeptide.

TypeIDPosition(s)Description
Signal1-85
ChainPRO_000041419286-3041Platelet binding protein GspB
Modified residue3041Pentaglycyl murein peptidoglycan amidated threonine
PropeptidePRO_00004141933042-3072Removed by sortase

Post-translational modification

Proteolytically cleaved by a metalloprotease.
Both SSR1 and SSR2 domains are glycosylated (Probable). A truncated derivative (residues 1-2062) contains 105 nmol per nmol of protein, suggesting at least 10% of the apparent molecular weight is due to carbohydrates (PubMed:14729688).
Glucose and N-acetylglucosamine are present in a ratio of 30:73 residues per truncated polypeptide, as well as minor amounts of galactose and N-acetylgalactosamine (PubMed:14729688).
Glycosylation occurs intracellularly in the Ser-rich regions SSR1 and SSR2 (PubMed:14729688, PubMed:15489421).
Glycosylation of SSR2 domain may be required to prevent aggregation of GspB (Probable). It is probable that most of the Ser residues in SSR1 and SSR2 are O-GlcNAcylated. Sequential glycosylation by sugar transferases are able to generate complex sugar polymorphisms (By similarity).

Keywords

Interaction

Subunit

Both SSR domains in the unglycosylated protein bind to Asp2 and Asp3; glycosylated protein binds less well. Interacts with the human cell surface glycoprotein GP1BA.

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q939N5asp2 Q9AET84EBI-6414561, EBI-6414583
BINARY Q939N5asp3 Q9AET74EBI-6414561, EBI-6414568

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for region, compositional bias, motif.

TypeIDPosition(s)Description
Region117-147Disordered
Region123-236Ser-rich region 1 (SSR1)
Compositional bias182-237Polar residues
Region182-254Disordered
Region237-603Basic region (BR)
Region604-3028Ser-rich region 2 (SSR2)
Region876-909Disordered
Region936-969Disordered
Region1024-2085Disordered
Region2106-2139Disordered
Region2173-2223Disordered
Region2250-2595Disordered
Region2625-2967Disordered
Compositional bias3014-3044Polar residues
Region3014-3045Disordered
Motif3038-3042LPXTG sorting signal

Domain

Has a short and long Ser-rich region with a basic region between them. The SRR domains themselves are comprised of inexact repeats of SASESASTSASV. SSR1 has 6 repeats, SSR2 has 200. The Ser-rich regions are both glycosylated. The basic region (BR) binds to whole cell lysates of wild-type but not bacteria deleted of this gene; it also recognizes whole cell lysates of S.aureus strain ISP479C probably via SraP, but not lysates of S.pneumoniae TIGR4 (PubMed:20714350).
The predicted pI of the basic region is 9.51 (PubMed:19202081).

Sequence similarities

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    3,072
  • Mass (Da)
    285,769
  • Last updated
    2001-12-01 v1
  • Checksum
    0B148372697CF7F2
MFFKRQKGQYHEVERVTRFKLIKSGKHWLRAATSQFGLLRLMKGSDVSSTEVKVVEEQSVEKSGLNYLKGIIATGAVLGGAVVTSSSVYAEEEQAHEKVIDTRDVLATRGEAVLSEEAATTLSSTEANPVESLSDTLSASESTSASSSVSTSISVSESFSVSGSLSYSTSLSQSVSASASASESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASSQTGRRRTRRAVTESAPNVEYHDVKGDMIQSVTTSFDDTSRLLTWTINLTPRQVKSNLGALVSISGNQETRTVTINGKNAANGGVYNSGGAWNLYTGESVNNNVLRITTQVNDTGGEVKLGLRLVTSDKKITKTNLPLEFSQVAATTNGSWDKAGYNTTIVEKDTERPVVNVPSEITVYRGESFEYFATVTDNSNAFDLAKTVVRWLYNNQPGRGTEWLQYSVTQVGNQLKVRIFGNVPIDTTIGDYTRYVVATDAAGNVNATQTEMGNAAVDKTSVNGQFKLIIRFRIKTPENTVFVNNPNQLTEVEKNLVREAVKKSNPDLRAQDVLNSNYVTGITVSNNGTTTITYRDGRKDIIDGSKFIDTRAGSISKSQSTSNSISVSLSKSESASASLVTSKLNSISSSASVSASTSISTSGSVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASTSASKSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESSSTSASVSASESSSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSTSVSTSTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASKSASTSESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASDSASISASVLASESASTSASVSASESASTSASVSASESASTSASVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASMSASTSASVSVSESTSTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASASASESASTSASVSASESASTSASVSASESASTSASVSASESASTNASVSVSESMSVSESLSLSISTSVLHSQLNDIYESELYSLSLSESLSASQSLSQSLSESQSSSASQSMHDRISKGQLPRTGESENKASILALGLGALGLAFKKRKKNESED

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias182-237Polar residues
Compositional bias3014-3044Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY028381
EMBL· GenBank· DDBJ
AAL13053.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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