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Q939N5 (GSPB_STRGN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Platelet binding protein GspB
Alternative name(s):
Serine-rich adhesin for platelets
Serine-rich repeat protein GspB
Gene names
Name:gspB
OrganismStreptococcus gordonii
Taxonomic identifier1302 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length3072 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Plays a role in virulence and host-pathogen interactions. Mediates binding to human platelets via interaction with the human cell surface glycoprotein GP1BA. Ref.6

Subunit structure

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. Ref.5 Ref.6

Subcellular location

Secretedcell wall; Peptidoglycan-anchor. Note: Exported by the accessory SecA2/SecY2 protein translocation apparatus. Ref.1 Ref.2

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.

Post-translational modification

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. Ref.2 Ref.4

Disruption phenotype

Loss of adherence to human platelet cells. Ref.1

Sequence similarities

Belongs to the SraP family.

Ontologies

Keywords
   Cellular componentCell wall
Secreted
   DomainSignal
   PTMGlycoprotein
Peptidoglycan-anchor
   Technical term3D-structure
Gene Ontology (GO)
   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 8585 Potential
Chain86 – 30412956Platelet binding protein GspB
PRO_0000414192
Propeptide3042 – 307231Removed by sortase Potential
PRO_0000414193

Regions

Region123 – 236114Ser-rich 1 (SSR1)
Region237 – 30272791Basic region (BR)
Region604 – 30282425Ser-rich 2 (SSR2)
Motif3038 – 30425LPXTG sorting signal Potential
Compositional bias123 – 236114Ser-rich
Compositional bias604 – 30282425Ser-rich
Compositional bias669 – 29632295Ala-rich

Sites

Site4431Important for interaction with host glycoprotein and virulence
Site4841Important for interaction with host glycoprotein and virulence
Site4851Important for interaction with host glycoprotein and virulence

Amino acid modifications

Modified residue30411Pentaglycyl murein peptidoglycan amidated threonine Potential

Experimental info

Mutagenesis4431Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. Ref.6
Mutagenesis4841R → E: Strongly reduced interaction with GP1BA carbohydrate chains. Strongly reduced platelet binding. Ref.6
Mutagenesis4851Y → F: Strongly reduced interaction with GP1BA carbohydrate chains. Ref.6

Secondary structure

.......................................................................... 3072
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q939N5 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 0B148372697CF7F2

FASTA3,072285,769
        10         20         30         40         50         60 
MFFKRQKGQY HEVERVTRFK LIKSGKHWLR AATSQFGLLR LMKGSDVSST EVKVVEEQSV 

        70         80         90        100        110        120 
EKSGLNYLKG IIATGAVLGG AVVTSSSVYA EEEQAHEKVI DTRDVLATRG EAVLSEEAAT 

       130        140        150        160        170        180 
TLSSTEANPV ESLSDTLSAS ESTSASSSVS TSISVSESFS VSGSLSYSTS LSQSVSASAS 

       190        200        210        220        230        240 
ASESLSVSSS ASDSVSASTS TSASASQSVS ASQKSTISTS ESTRSESSQQ STEASSQTGR 

       250        260        270        280        290        300 
RRTRRAVTES APNVEYHDVK GDMIQSVTTS FDDTSRLLTW TINLTPRQVK SNLGALVSIS 

       310        320        330        340        350        360 
GNQETRTVTI NGKNAANGGV YNSGGAWNLY TGESVNNNVL RITTQVNDTG GEVKLGLRLV 

       370        380        390        400        410        420 
TSDKKITKTN LPLEFSQVAA TTNGSWDKAG YNTTIVEKDT ERPVVNVPSE ITVYRGESFE 

       430        440        450        460        470        480 
YFATVTDNSN AFDLAKTVVR WLYNNQPGRG TEWLQYSVTQ VGNQLKVRIF GNVPIDTTIG 

       490        500        510        520        530        540 
DYTRYVVATD AAGNVNATQT EMGNAAVDKT SVNGQFKLII RFRIKTPENT VFVNNPNQLT 

       550        560        570        580        590        600 
EVEKNLVREA VKKSNPDLRA QDVLNSNYVT GITVSNNGTT TITYRDGRKD IIDGSKFIDT 

       610        620        630        640        650        660 
RAGSISKSQS TSNSISVSLS KSESASASLV TSKLNSISSS ASVSASTSIS TSGSVSASES 

       670        680        690        700        710        720 
ASTSSSVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASTSASKS 

       730        740        750        760        770        780 
ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASTSAS TSASVSASES 

       790        800        810        820        830        840 
ASTSASVSAS TSASTSASVS ASESASTSAS VSASTSASTS ASVSASASAS TSASVSASTS 

       850        860        870        880        890        900 
ASTSASVSAS ASASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES 

       910        920        930        940        950        960 
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASESASTS ASVSASESAS TSASVSASES 

       970        980        990       1000       1010       1020 
ASTSASVSAS ESASTSASVS ASTSASTSAS VSASTSASTS ASVSASTSAS TSASVSASTS 

      1030       1040       1050       1060       1070       1080 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASTSASTS ASVSASESAS TSASVSASES 

      1090       1100       1110       1120       1130       1140 
ASTSASESAS ESASTSASVS ASESASTSAS VSASESSSTS ASVSASESSS TSASVSASES 

      1150       1160       1170       1180       1190       1200 
ASTSASVSAS ESASTSASES ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1210       1220       1230       1240       1250       1260 
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES 

      1270       1280       1290       1300       1310       1320 
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1330       1340       1350       1360       1370       1380 
VSTSASVSAS ESASTSASVS ASESASTSAS ESASESASTS ASVSASESAS TSASVSASES 

      1390       1400       1410       1420       1430       1440 
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS 

      1450       1460       1470       1480       1490       1500 
ASTSASVSAS ESASTSTSVS TSTSASTSAS VSASESASTS ASVSASESAS TSASVSASTS 

      1510       1520       1530       1540       1550       1560 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASTS 

      1570       1580       1590       1600       1610       1620 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1630       1640       1650       1660       1670       1680 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1690       1700       1710       1720       1730       1740 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1750       1760       1770       1780       1790       1800 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1810       1820       1830       1840       1850       1860 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1870       1880       1890       1900       1910       1920 
ASTSASVSAS TSTSTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1930       1940       1950       1960       1970       1980 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      1990       2000       2010       2020       2030       2040 
ASTSASVSAS TSASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASES 

      2050       2060       2070       2080       2090       2100 
ASTSASVSAS ESASTSASVS ASESASTSAS VSASESASTS ASVSASESAS TSASVSASKS 

      2110       2120       2130       2140       2150       2160 
ASTSESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESVSTSASVS ASDSASISAS 

      2170       2180       2190       2200       2210       2220 
VLASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSSSVS ASESASTSAS 

      2230       2240       2250       2260       2270       2280 
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2290       2300       2310       2320       2330       2340 
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS 

      2350       2360       2370       2380       2390       2400 
VSASESASTS ASVSSSESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2410       2420       2430       2440       2450       2460 
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2470       2480       2490       2500       2510       2520 
VSASESASTS ASVSASTSAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS 

      2530       2540       2550       2560       2570       2580 
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2590       2600       2610       2620       2630       2640 
VSASESASTS ASVSASESAS TSASVSASMS ASTSASVSVS ESTSTSASVS ANESASTSAS 

      2650       2660       2670       2680       2690       2700 
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2710       2720       2730       2740       2750       2760 
VSASESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASTSASTSAS 

      2770       2780       2790       2800       2810       2820 
VSANESASTS ASVSASESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2830       2840       2850       2860       2870       2880 
VSASTSASTS ASVSANESAS TSASVSASES ASTSASVSAS ESASTSASVS ASESASTSAS 

      2890       2900       2910       2920       2930       2940 
VSASESASTS ASVSASTSAS TSASVSASES ASTSASASAS ESASTSASVS ASESASTSAS 

      2950       2960       2970       2980       2990       3000 
VSASESASTS ASVSASESAS TNASVSVSES MSVSESLSLS ISTSVLHSQL NDIYESELYS 

      3010       3020       3030       3040       3050       3060 
LSLSESLSAS QSLSQSLSES QSSSASQSMH DRISKGQLPR TGESENKASI LALGLGALGL 

      3070 
AFKKRKKNES ED 

« Hide

References

[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]"A structural model for binding of the serine-rich repeat adhesin GspB to host carbohydrate receptors."
Pyburn T.M., Bensing B.A., Xiong Y.Q., Melancon B.J., Tomasiak T.M., Ward N.J., Yankovskaya V., Oliver K.M., Cecchini G., Sulikowski G.A., Tyska M.J., Sullam P.M., Iverson T.M.
PLoS Pathog. 7:E1002112-E1002112(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY028381 Genomic DNA. Translation: AAL13053.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QC5X-ray1.40X245-604[»]
3QC6X-ray1.90X245-604[»]
4I8EX-ray1.90X233-617[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ939N5. 2 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR019948. Gram-positive_anchor.
IPR022263. KxYKxGKxW.
IPR019931. LPXTG_anchor.
IPR026465. Ser_adhes_glycop.
[Graphical view]
PfamPF00746. Gram_pos_anchor. 1 hit.
[Graphical view]
TIGRFAMsTIGR03715. KxYKxGKxW. 1 hit.
TIGR01167. LPXTG_anchor. 1 hit.
TIGR04224. ser_adhes_Nterm. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGSPB_STRGN
AccessionPrimary (citable) accession number: Q939N5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 14, 2011
Last sequence update: December 1, 2001
Last modified: February 19, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references