Q939N5 · GSPB_STRGN
- ProteinPlatelet binding protein GspB
- GenegspB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3072 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 443 | Important for interaction with host glycoprotein and virulence | ||||
Sequence: Y | ||||||
Site | 484 | Important for interaction with host glycoprotein and virulence | ||||
Sequence: R | ||||||
Site | 485 | Important for interaction with host glycoprotein and virulence | ||||
Sequence: Y |
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 | extracellular region | |
Biological Process | cell adhesion |
Keywords
- Biological process
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended namePlatelet binding protein GspB
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Bacillota > Bacilli > Lactobacillales > Streptococcaceae > Streptococcus
Accessions
- Primary accessionQ939N5
Subcellular Location
UniProt Annotation
GO Annotation
Secreted, cell wall ; Peptidoglycan-anchor
Note: Exported by the accessory SecA2/SecY2 protein translocation apparatus.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Loss of adherence to human platelet cells (PubMed:12010500).
Decrease in early biofilm formation (PubMed:20714350).
Decrease in early biofilm formation (PubMed:20714350).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 443 | Strongly reduced interaction with GP1BA carbohydrate chains. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 484 | Strongly reduced interaction with GP1BA carbohydrate chains. Strongly reduced platelet binding. | ||||
Sequence: R → E | ||||||
Mutagenesis | 485 | Strongly reduced interaction with GP1BA carbohydrate chains. | ||||
Sequence: Y → F |
PTM/Processing
Features
Showing features for signal, chain, modified residue, propeptide.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-85 | |||||
Sequence: MFFKRQKGQYHEVERVTRFKLIKSGKHWLRAATSQFGLLRLMKGSDVSSTEVKVVEEQSVEKSGLNYLKGIIATGAVLGGAVVTS | ||||||
Chain | PRO_0000414192 | 86-3041 | Platelet binding protein GspB | |||
Sequence: SSVYAEEEQAHEKVIDTRDVLATRGEAVLSEEAATTLSSTEANPVESLSDTLSASESTSASSSVSTSISVSESFSVSGSLSYSTSLSQSVSASASASESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASSQTGRRRTRRAVTESAPNVEYHDVKGDMIQSVTTSFDDTSRLLTWTINLTPRQVKSNLGALVSISGNQETRTVTINGKNAANGGVYNSGGAWNLYTGESVNNNVLRITTQVNDTGGEVKLGLRLVTSDKKITKTNLPLEFSQVAATTNGSWDKAGYNTTIVEKDTERPVVNVPSEITVYRGESFEYFATVTDNSNAFDLAKTVVRWLYNNQPGRGTEWLQYSVTQVGNQLKVRIFGNVPIDTTIGDYTRYVVATDAAGNVNATQTEMGNAAVDKTSVNGQFKLIIRFRIKTPENTVFVNNPNQLTEVEKNLVREAVKKSNPDLRAQDVLNSNYVTGITVSNNGTTTITYRDGRKDIIDGSKFIDTRAGSISKSQSTSNSISVSLSKSESASASLVTSKLNSISSSASVSASTSISTSGSVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASTSASKSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESSSTSASVSASESSSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSTSVSTSTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASKSASTSESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASDSASISASVLASESASTSASVSASESASTSASVSASESASTSASVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASMSASTSASVSVSESTSTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASASASESASTSASVSASESASTSASVSASESASTSASVSASESASTNASVSVSESMSVSESLSLSISTSVLHSQLNDIYESELYSLSLSESLSASQSLSQSLSESQSSSASQSMHDRISKGQLPRT | ||||||
Modified residue | 3041 | Pentaglycyl murein peptidoglycan amidated threonine | ||||
Sequence: T | ||||||
Propeptide | PRO_0000414193 | 3042-3072 | Removed by sortase | |||
Sequence: GESENKASILALGLGALGLAFKKRKKNESED |
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).
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
- PTM
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
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q939N5 | asp2 Q9AET8 | 4 | EBI-6414561, EBI-6414583 | |
BINARY | Q939N5 | asp3 Q9AET7 | 4 | EBI-6414561, EBI-6414568 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 117-147 | Disordered | ||||
Sequence: EAATTLSSTEANPVESLSDTLSASESTSASS | ||||||
Region | 123-236 | Ser-rich region 1 (SSR1) | ||||
Sequence: SSTEANPVESLSDTLSASESTSASSSVSTSISVSESFSVSGSLSYSTSLSQSVSASASASESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASS | ||||||
Compositional bias | 182-237 | Polar residues | ||||
Sequence: SESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASSQ | ||||||
Region | 182-254 | Disordered | ||||
Sequence: SESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASSQTGRRRTRRAVTESAPNV | ||||||
Region | 237-603 | Basic region (BR) | ||||
Sequence: QTGRRRTRRAVTESAPNVEYHDVKGDMIQSVTTSFDDTSRLLTWTINLTPRQVKSNLGALVSISGNQETRTVTINGKNAANGGVYNSGGAWNLYTGESVNNNVLRITTQVNDTGGEVKLGLRLVTSDKKITKTNLPLEFSQVAATTNGSWDKAGYNTTIVEKDTERPVVNVPSEITVYRGESFEYFATVTDNSNAFDLAKTVVRWLYNNQPGRGTEWLQYSVTQVGNQLKVRIFGNVPIDTTIGDYTRYVVATDAAGNVNATQTEMGNAAVDKTSVNGQFKLIIRFRIKTPENTVFVNNPNQLTEVEKNLVREAVKKSNPDLRAQDVLNSNYVTGITVSNNGTTTITYRDGRKDIIDGSKFIDTRAG | ||||||
Region | 604-3028 | Ser-rich region 2 (SSR2) | ||||
Sequence: SISKSQSTSNSISVSLSKSESASASLVTSKLNSISSSASVSASTSISTSGSVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASTSASKSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASASASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESSSTSASVSASESSSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSTSVSTSTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASKSASTSESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASDSASISASVLASESASTSASVSASESASTSASVSASESASTSASVSASESASTSSSVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASMSASTSASVSVSESTSTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASASASESASTSASVSASESASTSASVSASESASTSASVSASESASTNASVSVSESMSVSESLSLSISTSVLHSQLNDIYESELYSLSLSESLSASQSLSQSLSESQSSSASQS | ||||||
Region | 876-909 | Disordered | ||||
Sequence: SASTSASVSASESASTSASVSASESASTSASVSA | ||||||
Region | 936-969 | Disordered | ||||
Sequence: SASTSASVSASESASTSASVSASESASTSASVSA | ||||||
Region | 1024-2085 | Disordered | ||||
Sequence: SASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESSSTSASVSASESSSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESVSTSASVSASESASTSASVSASESASTSASESASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSTSVSTSTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSTSTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSA | ||||||
Region | 2106-2139 | Disordered | ||||
Sequence: SASTSASVSASESASTSASVSASESASTSASVSA | ||||||
Region | 2173-2223 | Disordered | ||||
Sequence: VSASESASTSASVSASESASTSASVSASESASTSSSVSASESASTSASVSA | ||||||
Region | 2250-2595 | Disordered | ||||
Sequence: SASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSSSESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSA | ||||||
Region | 2625-2967 | Disordered | ||||
Sequence: TSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSANESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASESASTSASVSASTSASTSASVSASESASTSASASASESASTSASVSASESASTSASVSASESASTSASVSASESASTNASVSV | ||||||
Compositional bias | 3014-3044 | Polar residues | ||||
Sequence: SQSLSESQSSSASQSMHDRISKGQLPRTGES | ||||||
Region | 3014-3045 | Disordered | ||||
Sequence: SQSLSESQSSSASQSMHDRISKGQLPRTGESE | ||||||
Motif | 3038-3042 | LPXTG sorting signal | ||||
Sequence: LPRTG |
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).
The predicted pI of the basic region is 9.51 (PubMed:19202081).
Sequence similarities
Belongs to the serine-rich repeat protein (SRRP) family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length3,072
- Mass (Da)285,769
- Last updated2001-12-01 v1
- Checksum0B148372697CF7F2
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 182-237 | Polar residues | ||||
Sequence: SESLSVSSSASDSVSASTSTSASASQSVSASQKSTISTSESTRSESSQQSTEASSQ | ||||||
Compositional bias | 3014-3044 | Polar residues | ||||
Sequence: SQSLSESQSSSASQSMHDRISKGQLPRTGES |
Keywords
- Technical term