Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q939N5

- GSPB_STRGN

UniProt

Q939N5 - GSPB_STRGN

(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)

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

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-KW
  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 – 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

        10         20         30         40         50
MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST
60 70 80 90 100
EVKVVEEQSV EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI
110 120 130 140 150
DTRDVLATRG EAVLSEEAAT TLSSTEANPV ESLSDTLSAS ESTSASSSVS
160 170 180 190 200
TSISVSESFS VSGSLSYSTS LSQSVSASAS ASESLSVSSS ASDSVSASTS
210 220 230 240 250
TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR RRTRRAVTES
260 270 280 290 300
APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS
310 320 330 340 350
GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG
360 370 380 390 400
GEVKLGLRLV TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT
410 420 430 440 450
ERPVVNVPSE ITVYRGESFE YFATVTDNSN AFDLAKTVVR WLYNNQPGRG
460 470 480 490 500
TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG DYTRYVVATD AAGNVNATQT
510 520 530 540 550
EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT EVEKNLVREA
560 570 580 590 600
VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT
610 620 630 640 650
RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS
660 670 680 690 700
TSGSVSASES ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS
710 720 730 740 750
ASVSASTSAS TSASTSASKS ASTSASVSAS TSASTSASVS ASESASTSAS
760 770 780 790 800
VSASTSASTS ASVSASTSAS TSASVSASES ASTSASVSAS TSASTSASVS
810 820 830 840 850
ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS ASTSASVSAS
860 870 880 890 900
ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
910 920 930 940 950
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS
960 970 980 990 1000
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS
1010 1020 1030 1040 1050
ASVSASTSAS TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS
1060 1070 1080 1090 1100
VSASTSASTS ASVSASESAS TSASVSASES ASTSASESAS ESASTSASVS
1110 1120 1130 1140 1150
ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES ASTSASVSAS
1160 1170 1180 1190 1200
ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
1210 1220 1230 1240 1250
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS
1260 1270 1280 1290 1300
TSASVSASES ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS
1310 1320 1330 1340 1350
ASVSASESAS TSASVSASES VSTSASVSAS ESASTSASVS ASESASTSAS
1360 1370 1380 1390 1400
ESASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS
1410 1420 1430 1440 1450
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS ASTSASVSAS
1460 1470 1480 1490 1500
ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS
1510 1520 1530 1540 1550
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
1560 1570 1580 1590 1600
TSASVSASTS ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS
1610 1620 1630 1640 1650
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
1660 1670 1680 1690 1700
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS
1710 1720 1730 1740 1750
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
1760 1770 1780 1790 1800
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES
1810 1820 1830 1840 1850
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
1860 1870 1880 1890 1900
TSASVSASES ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS
1910 1920 1930 1940 1950
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
1960 1970 1980 1990 2000
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS TSASTSASVS
2010 2020 2030 2040 2050
ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2060 2070 2080 2090 2100
ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS
2110 2120 2130 2140 2150
ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS
2160 2170 2180 2190 2200
ASDSASISAS VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2210 2220 2230 2240 2250
ESASTSSSVS ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES
2260 2270 2280 2290 2300
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
2310 2320 2330 2340 2350
TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS
2360 2370 2380 2390 2400
ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
2410 2420 2430 2440 2450
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS
2460 2470 2480 2490 2500
ASESASTSAS VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS
2510 2520 2530 2540 2550
ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES
2560 2570 2580 2590 2600
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS
2610 2620 2630 2640 2650
TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS VSASESASTS
2660 2670 2680 2690 2700
ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS
2710 2720 2730 2740 2750
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS
2760 2770 2780 2790 2800
ASTSASTSAS VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS
2810 2820 2830 2840 2850
ESASTSASVS ASESASTSAS VSASTSASTS ASVSANESAS TSASVSASES
2860 2870 2880 2890 2900
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASTSAS
2910 2920 2930 2940 2950
TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS VSASESASTS
2960 2970 2980 2990 3000
ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS
3010 3020 3030 3040 3050
LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI
3060 3070
LALGLGALGL AFKKRKKNES ED
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 29, 2014
This is version 49 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