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Q939N5

- GSPB_STRGN

UniProt

Q939N5 - GSPB_STRGN

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Protein
Platelet binding protein GspB
Gene
gspB
Organism
Streptococcus gordonii
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei443 – 4431Important for interaction with host glycoprotein and virulence
Sitei484 – 4841Important for interaction with host glycoprotein and virulence
Sitei485 – 4851Important for interaction with host glycoprotein and virulence

GO - Molecular functioni

  1. protein binding Source: IntAct
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Platelet binding protein GspB
Alternative name(s):
Serine-rich adhesin for platelets
Serine-rich repeat protein GspB
Gene namesi
Name:gspB
OrganismiStreptococcus gordonii
Taxonomic identifieri1302 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Subcellular locationi

Secretedcell wall; Peptidoglycan-anchor
Note: Exported by the accessory SecA2/SecY2 protein translocation apparatus.2 Publications

GO - Cellular componenti

  1. cell wall Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Disruption phenotypei

Loss of adherence to human platelet cells.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi443 – 4431Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. 1 Publication
Mutagenesisi484 – 4841R → E: Strongly reduced interaction with GP1BA carbohydrate chains. Strongly reduced platelet binding. 1 Publication
Mutagenesisi485 – 4851Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 8585 Reviewed prediction
Add
BLAST
Chaini86 – 30412956Platelet binding protein GspB
PRO_0000414192Add
BLAST
Propeptidei3042 – 307231Removed by sortase Reviewed prediction
PRO_0000414193Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3041 – 30411Pentaglycyl murein peptidoglycan amidated threonine Reviewed prediction

Post-translational modificationi

Proteolytically cleaved by a metalloprotease By similarity.
Both SSR1 and SSR2 domains are glycosylated. A truncated derivative (about residues 1-2062) contains 105 nmol per nmol of protein, suggesting at least 10% of the apparent molecular weight is due to carbohydrates. 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. Glycosylation occurs intracellularly in the Ser-rich regions SSR1 and SSR2. Glycosylation of SSR2 domain may be required to prevent aggregation of GspB.2 Publications

Keywords - PTMi

Glycoprotein, Peptidoglycan-anchor

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
asp2Q9AET84EBI-6414561,EBI-6414583
asp3Q9AET74EBI-6414561,EBI-6414568

Protein-protein interaction databases

IntActiQ939N5. 2 interactions.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi247 – 2504
Beta strandi253 – 2575
Beta strandi263 – 27210
Turni273 – 2753
Beta strandi277 – 2848
Beta strandi291 – 2999
Beta strandi303 – 3108
Beta strandi316 – 3194
Beta strandi322 – 3254
Beta strandi328 – 3336
Beta strandi338 – 3469
Beta strandi351 – 36414
Turni368 – 3703
Helixi375 – 3773
Turni379 – 3824
Beta strandi386 – 39510
Beta strandi404 – 4063
Beta strandi409 – 4146
Beta strandi418 – 4269
Beta strandi432 – 4409
Beta strandi442 – 4476
Beta strandi455 – 4617
Beta strandi464 – 4729
Beta strandi475 – 4773
Beta strandi480 – 49011
Beta strandi495 – 4973
Helixi499 – 50810
Beta strandi515 – 5217
Beta strandi531 – 5344
Helixi541 – 55414
Helixi560 – 5623
Helixi564 – 5663
Helixi568 – 5714
Beta strandi572 – 5743
Beta strandi580 – 5845
Beta strandi589 – 5924
Turni595 – 5973
Beta strandi598 – 6014

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3QC5X-ray1.40X245-604[»]
3QC6X-ray1.90X245-604[»]
4I8EX-ray1.90X233-617[»]

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni123 – 236114Ser-rich 1 (SSR1)
Add
BLAST
Regioni237 – 30272791Basic region (BR)
Add
BLAST
Regioni604 – 30282425Ser-rich 2 (SSR2)
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi3038 – 30425LPXTG sorting signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi123 – 236114Ser-rich
Add
BLAST
Compositional biasi604 – 30282425Ser-rich
Add
BLAST
Compositional biasi669 – 29632295Ala-rich
Add
BLAST

Domaini

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.

Sequence similaritiesi

Belongs to the SraP family.

Keywords - Domaini

Signal

Family and domain databases

InterProiIPR019948. Gram-positive_anchor.
IPR022263. KxYKxGKxW.
IPR019931. LPXTG_anchor.
IPR026465. Ser_adhes_glycop.
[Graphical view]
PfamiPF00746. Gram_pos_anchor. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03715. KxYKxGKxW. 1 hit.
TIGR01167. LPXTG_anchor. 1 hit.
TIGR04224. ser_adhes_Nterm. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q939N5-1 [UniParc]FASTAAdd to Basket

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MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST     50
EVKVVEEQSV EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI 100
DTRDVLATRG EAVLSEEAAT TLSSTEANPV ESLSDTLSAS ESTSASSSVS 150
TSISVSESFS VSGSLSYSTS LSQSVSASAS ASESLSVSSS ASDSVSASTS 200
TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR RRTRRAVTES 250
APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS 300
GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG 350
GEVKLGLRLV TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT 400
ERPVVNVPSE ITVYRGESFE YFATVTDNSN AFDLAKTVVR WLYNNQPGRG 450
TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG DYTRYVVATD AAGNVNATQT 500
EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT EVEKNLVREA 550
VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT 600
RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS 650
TSGSVSASES ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS 700
ASVSASTSAS TSASTSASKS ASTSASVSAS TSASTSASVS ASESASTSAS 750
VSASTSASTS ASVSASTSAS TSASVSASES ASTSASVSAS TSASTSASVS 800
ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS ASTSASVSAS 850
ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES 900
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS 950
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS 1000
ASVSASTSAS TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS 1050
VSASTSASTS ASVSASESAS TSASVSASES ASTSASESAS ESASTSASVS 1100
ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES ASTSASVSAS 1150
ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 1200
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS 1250
TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS 1300
ASVSASESAS TSASVSASES VSTSASVSAS ESASTSASVS ASESASTSAS 1350
ESASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS 1400
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS ASTSASVSAS 1450
ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS 1500
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS 1550
TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS 1600
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 1650
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS 1700
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS 1750
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 1800
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS 1850
TSASVSASES ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS 1900
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 1950
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS 2000
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS 2050
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS 2100
ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS 2150
ASDSASISAS VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS 2200
ESASTSSSVS ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES 2250
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS 2300
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS 2350
ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 2400
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS 2450
ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS 2500
ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES 2550
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS 2600
TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS VSASESASTS 2650
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 2700
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS 2750
ASTSASTSAS VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS 2800
ESASTSASVS ASESASTSAS VSASTSASTS ASVSANESAS TSASVSASES 2850
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASTSAS 2900
TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS VSASESASTS 2950
ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS 3000
LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI 3050
LALGLGALGL AFKKRKKNES ED 3072
Length:3,072
Mass (Da):285,769
Last modified:December 1, 2001 - v1
Checksum:i0B148372697CF7F2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028381 Genomic DNA. Translation: AAL13053.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028381 Genomic DNA. Translation: AAL13053.1 .

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3QC5 X-ray 1.40 X 245-604 [» ]
3QC6 X-ray 1.90 X 245-604 [» ]
4I8E X-ray 1.90 X 233-617 [» ]
ModBasei Search...

Protein-protein interaction databases

IntActi Q939N5. 2 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR019948. Gram-positive_anchor.
IPR022263. KxYKxGKxW.
IPR019931. LPXTG_anchor.
IPR026465. Ser_adhes_glycop.
[Graphical view ]
Pfami PF00746. Gram_pos_anchor. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR03715. KxYKxGKxW. 1 hit.
TIGR01167. LPXTG_anchor. 1 hit.
TIGR04224. ser_adhes_Nterm. 1 hit.
ProtoNeti Search...

Publicationsi

  1. "An accessory sec locus of Streptococcus gordonii is required for export of the surface protein GspB and for normal levels of binding to human platelets."
    Bensing B.A., Sullam P.M.
    Mol. Microbiol. 44:1081-1094(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.
    Strain: M99.
  2. "The Streptococcus gordonii platelet binding protein GspB undergoes glycosylation independently of export."
    Bensing B.A., Gibson B.W., Sullam P.M.
    J. Bacteriol. 186:638-645(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION, SUBCELLULAR LOCATION.
    Strain: M99.
  3. "Genes in the accessory sec locus of Streptococcus gordonii have three functionally distinct effects on the expression of the platelet-binding protein GspB."
    Takamatsu D., Bensing B.A., Sullam P.M.
    Mol. Microbiol. 52:189-203(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: EXPORT VIA THE ACCESSORY SECA2/SECY2 SYSTEM.
    Strain: M99.
  4. "Four proteins encoded in the gspB-secY2A2 operon of Streptococcus gordonii mediate the intracellular glycosylation of the platelet-binding protein GspB."
    Takamatsu D., Bensing B.A., Sullam P.M.
    J. Bacteriol. 186:7100-7111(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION OF SER-RICH REGIONS.
    Strain: M99.
  5. "Asp2 and Asp3 interact directly with GspB, the export substrate of the Streptococcus gordonii accessory Sec System."
    Yen Y.T., Seepersaud R., Bensing B.A., Sullam P.M.
    J. Bacteriol. 193:3165-3174(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ASP2 AND ASP3.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) OF 245-604, FUNCTION, MUTAGENESIS OF TYR-443; ARG-484 AND TYR-485, INTERACTION WITH HUMAN GP1BA.

Entry informationi

Entry nameiGSPB_STRGN
AccessioniPrimary (citable) accession number: Q939N5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: December 1, 2001
Last modified: June 11, 2014
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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