A8AUS0 · SSPA_STRGC
- ProteinStreptococcal surface protein A
- GenesspA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1575 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
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).
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cell surface | |
Cellular Component | extracellular region |
Keywords
- Biological process
Names & Taxonomy
Protein names
- Recommended nameStreptococcal surface protein A
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionA8AUS0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Secreted, cell wall ; Peptidoglycan-anchor
Cell surface ; Peptidoglycan-anchor
Keywords
- Cellular component
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).
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
- Disease
PTM/Processing
Features
Showing features for signal, chain, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-38 | |||||
Sequence: MNKRKEVFGFRKSKVAKTLCGAVLGAALIAIADQQVLA | ||||||
Chain | PRO_5002717652 | 39-1575 | Streptococcal surface protein A | |||
Sequence: DEVTETNSTANVAVTTTGNPATNLPEAQGEATEAASQSQAQAGSKEGALPVEVSADDLNQAVTDAKAAGVNVVQDQTSDKGTATTAAENAQKQAEIKSDYAKQAEEIKKTTEAYKKEVEAHQAETDKINAENKAAEDKYQEDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKANEDSQLDYQNKLSAYQAELARVQKANAEAKEAYEKAVKENTAKNAALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAKEDNDADYQAKLAAYQAELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAIKQRNAAAKATYEAALKQYEADLAAAKKANEDSDADYQAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQAENEEIKQRNAAAKTDYEAKLAKYEADLAKYKKELAEYPAKLKAYEDEQAQIKAALVELEKNKNQDGYLSKPSAQSLVYDSEPNAQLSLTTNGKMLKASAVDEAFSHDTAQYSKKILQPDNLNVSYLQQADDVTSSMELYGNFGDKAGWTTTVGNNTEVKFASVLLERGQSVTATYTNLEKSYYNGKKISKVVFKYTLDSDSKFKNVDKAWLGVFTDPTLGVFASAYTGQEEKDTSIFIKNEFTFYDENDQPINFDNALLSVASLNRENNSIEMAKDYSGTFVKISGSSVGEKDGKIYATETLNFKQGQGGSRWTMYKNSQPGSGWDSSDAPNSWYGAGAISMSGPTNHVTVGAISATQVVPSDPVMAVATGKRPNIWYSLNGKIRAVNVPKITKEKPTPPVAPTEPQAPTYEVEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVVPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYDPLPTPPVAPTPKQLPTPPVVPTVHFHYSSLLAQPQINKEIKNEDGVDIDRTLVAKQSIVKFELKTEALTAGRPKTTSFVLVDPLPTGYKFDLDATKAASTGFDTTYDEASHTVTFKATDETLATYNADLTKPVETLHPTVVGRVLNDGATYTNNFTLTVNDAYGIKSNVVRVTTPGKPNDPDNPNNNYIKPTKVNKNKEGLNIDGKEVLAGSTNYYELTWDLDQYKGDKSSKEAIQNGFYYVDDYPEEALDVRPDLVKVADEKGNQVSGVSVQQYDSLEAAPKKVQDLLKKANITVKGAFQLFSADNPEEFYKQYVSTGTSLVITDPMTVKSEFGKTGGKYENKAYQIDFGNGYATEVVVNNVPKITPKKDVTVSLDPTSENLDGQTVQLYQTFNYRLIGGLIPQNHSEELEDYSFVDDYDQAGDQYTGNYKTFSSLNLTMKDGSVIKAGTDLTSQTTAETDAANGIVTVRFKEDFLQKISLDSPFQAETYLQMRRIAIGTFENTYVNTVNKVAYASNTVRTTTPIPRTPDKPTPIPTPKPKDPDKPETPKEPKVPSPKVEDPSAPIPVSVGKELTTLPKTGTNDSSYMPYLGLAALVGVLGLGQLKRKEDESN | ||||||
Modified residue | 1542 | Pentaglycyl murein peptidoglycan amidated threonine | ||||
Sequence: T | ||||||
Propeptide | PRO_5018350862 | 1543-1575 | Removed by sortase | |||
Sequence: GTNDSSYMPYLGLAALVGVLGLGQLKRKEDESN |
Keywords
- PTM
Expression
Induction
Induced by growth in the presence of collagen (at protein level).
Interaction
Structure
Family & Domains
Features
Showing features for compositional bias, region, repeat, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-82 | Polar residues | ||||
Sequence: VTTTGNPATNLPEAQGEATEAASQSQAQAGS | ||||||
Region | 52-86 | Disordered | ||||
Sequence: VTTTGNPATNLPEAQGEATEAASQSQAQAGSKEGA | ||||||
Repeat | 146-220 | Ag I/II A 1 | ||||
Sequence: KKTTEAYKKEVEAHQAETDKINAENKAAEDKYQEDLKAHQAEVEKINTANATAKAEYEAKLAQYQKDLAAVQKAN | ||||||
Repeat | 221-302 | Ag I/II A 2 | ||||
Sequence: EDSQLDYQNKLSAYQAELARVQKANAEAKEAYEKAVKENTAKNAALQAENEAIKQRNETAKANYDAAMKQYEADLAAIKKAK | ||||||
Repeat | 303-384 | Ag I/II A 3 | ||||
Sequence: EDNDADYQAKLAAYQAELARVQKANADAKAAYEKAVEENTAKNTAIQAENEAIKQRNAAAKATYEAALKQYEADLAAAKKAN | ||||||
Repeat | 385-466 | Ag I/II A 4 | ||||
Sequence: EDSDADYQAKLAAYQTELARVQKANADAKAAYEKAVEDNKAKNAALQAENEEIKQRNAAAKTDYEAKLAKYEADLAKYKKEL | ||||||
Region | 823-978 | Disordered | ||||
Sequence: KITKEKPTPPVAPTEPQAPTYEVEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVVPTYENEPTPPVKTPDQPEPSKPEEPTYETEKPLEPAPVAPTYENEPTPPVKTPDQPEPSKPEEPTYDPLPTPPVAPTPKQLPTP | ||||||
Compositional bias | 855-871 | Pro residues | ||||
Sequence: APTYENEPTPPVKTPDQ | ||||||
Compositional bias | 894-910 | Pro residues | ||||
Sequence: VPTYENEPTPPVKTPDQ | ||||||
Compositional bias | 933-949 | Pro residues | ||||
Sequence: APTYENEPTPPVKTPDQ | ||||||
Compositional bias | 956-978 | Pro residues | ||||
Sequence: EEPTYDPLPTPPVAPTPKQLPTP | ||||||
Region | 1482-1548 | Disordered | ||||
Sequence: RTTTPIPRTPDKPTPIPTPKPKDPDKPETPKEPKVPSPKVEDPSAPIPVSVGKELTTLPKTGTNDSS | ||||||
Compositional bias | 1499-1519 | Basic and acidic residues | ||||
Sequence: TPKPKDPDKPETPKEPKVPSP | ||||||
Motif | 1539-1543 | LPXTG sorting signal | ||||
Sequence: LPKTG |
Sequence similarities
Belongs to the antigen I/II family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,575
- Mass (Da)171,926
- Last updated2007-10-23 v1
- Checksum5F9EA5F22CC2278D
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 52-82 | Polar residues | ||||
Sequence: VTTTGNPATNLPEAQGEATEAASQSQAQAGS | ||||||
Compositional bias | 855-871 | Pro residues | ||||
Sequence: APTYENEPTPPVKTPDQ | ||||||
Compositional bias | 894-910 | Pro residues | ||||
Sequence: VPTYENEPTPPVKTPDQ | ||||||
Compositional bias | 933-949 | Pro residues | ||||
Sequence: APTYENEPTPPVKTPDQ | ||||||
Compositional bias | 956-978 | Pro residues | ||||
Sequence: EEPTYDPLPTPPVAPTPKQLPTP | ||||||
Compositional bias | 1499-1519 | Basic and acidic residues | ||||
Sequence: TPKPKDPDKPETPKEPKVPSP |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000725 EMBL· GenBank· DDBJ | ABV10916.1 EMBL· GenBank· DDBJ | Genomic DNA |