A8AUS0 · SSPA_STRGC

Function

function

Adhesin that mediates binding of bacteria to a variety of host cells. Plays a role in the bacterial invasion of dentinal tubules (PubMed:9393810).
A host immunostimulatory component, it modulates the innate immunity response. Plays a protective role against some antibiotics and cationic antimicrobial peptides (histatin-5, HTN3, but not beta-defensin 4A, DEFB4A). Purified soluble protein stimulates human epithelial cells to produce IL-6 and monocyte chemotactic protein (MCP-1, CCL2) probably via interaction with integrin beta-1 (ITGB1) (PubMed:22609749).

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).

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 Componentcell surface
Cellular Componentextracellular region

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Streptococcal surface protein A
  • Alternative names
    • Adhesin SspS

Gene names

    • Name
      sspA
    • Ordered locus names
      SGO_0210

Organism names

Accessions

  • Primary accession
    A8AUS0

Proteomes

Subcellular Location

Secreted, cell wall
; Peptidoglycan-anchor
Cell surface
; Peptidoglycan-anchor

Keywords

Phenotypes & Variants

Disruption phenotype

Single sspA deletion, bacteria invade human dental roots less well, adhere less well to collagen, decreased accumulation of mature SspB; double sspA-sspB deletion, no invasion of dental roots, collagen adherence is further reduced, as is chaining on soluble collagen (PubMed:9393810).
Triple sspA-sspB-hsa deletion no longer causes human platelet aggregation; double sspA-sspB deletion still causes platelet aggregation (PubMed:19884334).
Double sspA-sspB adheres better to human epithelial cells and is internalized better than wild-type cells, but induces less host cytokine production (IL-6, IL-8, monocyte chemotactic protein). Stimulates less cytokine production in mouse bone marrow-derived dendritic cells (IL-6, IL-10, IL-12, tumor necrosis factor). Increased sensitivity to antibiotics polymyxin B and nisin, and human histatin-5 (His3-(20-43)-peptide, HTN3). In intranasal mouse infection, the double mutant is cleared less quickly from lungs, neutrophil, hemokine and cytokine production are delayed or reduced (PubMed:22609749).

Keywords

PTM/Processing

Features

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

TypeIDPosition(s)Description
Signal1-38
ChainPRO_500271765239-1575Streptococcal surface protein A
Modified residue1542Pentaglycyl murein peptidoglycan amidated threonine
PropeptidePRO_50183508621543-1575Removed by sortase

Keywords

Expression

Induction

Induced by growth in the presence of collagen (at protein level).

Interaction

Subunit

Binds to human integrin beta-1 (ITGB1).

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for compositional bias, region, repeat, motif.

TypeIDPosition(s)Description
Compositional bias52-82Polar residues
Region52-86Disordered
Repeat146-220Ag I/II A 1
Repeat221-302Ag I/II A 2
Repeat303-384Ag I/II A 3
Repeat385-466Ag I/II A 4
Region823-978Disordered
Compositional bias855-871Pro residues
Compositional bias894-910Pro residues
Compositional bias933-949Pro residues
Compositional bias956-978Pro residues
Region1482-1548Disordered
Compositional bias1499-1519Basic and acidic residues
Motif1539-1543LPXTG sorting signal

Sequence similarities

Belongs to the antigen I/II family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Sequence processing
    The displayed sequence is further processed into a mature form.
  • Length
    1,575
  • Mass (Da)
    171,926
  • Last updated
    2007-10-23 v1
  • Checksum
    5F9EA5F22CC2278D
MNKRKEVFGFRKSKVAKTLCGAVLGAALIAIADQQVLADEVTETNSTANVAVTTTGNPATNLPEAQGEATEAASQSQAQAGSKEGALPVEVSADDLNQAVTDAKAAGVNVVQDQTSDKGTATTAAENAQKQAEIKSDYAKQAEEIKKTTEAYKKEVEAHQAETDKINAENKAAEDKYQEDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKANEDSQLDYQNKLSAYQAELARVQKANAEAKEAYEKAVKENTAKNAALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQAELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAIKQRNAAAKATYEAALKQYEADLAAAKKANEDSDADYQAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQAENEEIKQRNAAAKTDYEAKLAKYEADLAKYKKELAEYPAKLKAYEDEQAQIKAALVELEKNKNQDGYLSKPSAQSLVYDSEPNAQLSLTTNGKMLKASAVDEAFSHDTAQYSKKILQPDNLNVSYLQQADDVTSSMELYGNFGDKAGWTTTVGNNTEVKFASVLLERGQSVTATYTNLEKSYYNGKKISKVVFKYTLDSDSKFKNVDKAWLGVFTDPTLGVFASAYTGQEEKDTSIFIKNEFTFYDENDQPINFDNALLSVASLNRENNSIEMAKDYSGTFVKISGSSVGEKDGKIYATETLNFKQGQGGSRWTMYKNSQPGSGWDSSDAPNSWYGAGAISMSGPTNHVTVGAISATQVVPSDPVMAVATGKRPNIWYSLNGKIRAVNVPKITKEKPTPPVAPTEPQAPTYEVEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVVPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYDPLPTPPVAPTPKQLPTPPVVPTVHFHYSSLLAQPQINKEIKNEDGVDIDRTLVAKQSIVKFELKTEALTAGRPKTTSFVLVDPLPTGYKFDLDATKAASTGFDTTYDEASHTVTFKATDETLATYNADLTKPVETLHPTVVGRVLNDGATYTNNFTLTVNDAYGIKSNVVRVTTPGKPNDPDNPNNNYIKPTKVNKNKEGLNIDGKEVLAGSTNYYELTWDLDQYKGDKSSKEAIQNGFYYVDDYPEEALDVRPDLVKVADEKGNQVSGVSVQQYDSLEAAPKKVQDLLKKANITVKGAFQLFSADNPEEFYKQYVSTGTSLVITDPMTVKSEFGKTGGKYENKAYQIDFGNGYATEVVVNNVPKITPKKDVTVSLDPTSENLDGQTVQLYQTFNYRLIGGLIPQNHSEELEDYSFVDDYDQAGDQYTGNYKTFSSLNLTMKDGSVIKAGTDLTSQTTAETDAANGIVTVRFKEDFLQKISLDSPFQAETYLQMRRIAIGTFENTYVNTVNKVAYASNTVRTTTPIPRTPDKPTPIPTPKPKDPDKPETPKEPKVPSPKVEDPSAPIPVSVGKELTTLPKTGTNDSSYMPYLGLAALVGVLGLGQLKRKEDESN

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias52-82Polar residues
Compositional bias855-871Pro residues
Compositional bias894-910Pro residues
Compositional bias933-949Pro residues
Compositional bias956-978Pro residues
Compositional bias1499-1519Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000725
EMBL· GenBank· DDBJ
ABV10916.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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