Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q939N5

- GSPB_STRGN

UniProt

Q939N5 - GSPB_STRGN

Protein

Platelet binding protein GspB

Gene

gspB

Organism
Streptococcus gordonii
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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

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

    GO - Cellular componenti

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

    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 – 8585Sequence AnalysisAdd
    BLAST
    Chaini86 – 30412956Platelet binding protein GspBPRO_0000414192Add
    BLAST
    Propeptidei3042 – 307231Removed by sortaseSequence AnalysisPRO_0000414193Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei3041 – 30411Pentaglycyl murein peptidoglycan amidated threonineSequence Analysis

    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

    1
    3072
    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[»]
    ModBaseiSearch...
    MobiDBiSearch...

    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 signalSequence Analysis

    Compositional bias

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

    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

    « Hide

    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...
    MobiDBi 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: October 1, 2014
    This is version 48 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