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Q9EYW6 (SSPC_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 74. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Staphostatin B
Alternative name(s):
Staphylococcal cysteine protease B inhibitor
Gene names
Name:sspC
Ordered Locus Names:SAOUHSC_00986
OrganismStaphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length109 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically inhibits the cysteine protease staphopain B (SspB) by blocking the active site of the enzyme. Probably required to protect cytoplasmic proteins from being degraded by prematurely activated/folded prostaphopain B. Also involved in growth capacity, viability and bacterial morphology. Ref.3 Ref.7

Subunit structure

Forms a stable non-covalent complex with prematurely activated/folded SspB.

Subcellular location

Cytoplasm Ref.3.

Induction

Expression occurs in a growth-phase-dependent manner with optimal expression at post-exponential phase. Up-regulated by Agr (accessory gene regulator) and repressed by SarA (staphylococcal accessory regulator) and sigmaB factor. Ref.4 Ref.6

Miscellaneous

Inactivated by staphylococcal serine protease (SspA).

Disruption of sspC causes a total loss of secreted extracellular proteins and a partial loss of peptidoglycan-associated proteins. Loss of SspC results in profoundly reduced susceptibility of peptidoglycan to lysis by lysostaphin.

Sequence similarities

Belongs to the protease inhibitor I57 (SspC) family. [View classification]

Ontologies

Keywords
   Biological processVirulence
   Cellular componentCytoplasm
   Molecular functionProtease inhibitor
Thiol protease inhibitor
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processpathogenesis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncysteine-type endopeptidase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 109109Staphostatin B
PRO_0000220553

Regions

Region97 – 1015Binds to staphopain B

Experimental info

Mutagenesis981G → A or R: Loss of affinity for SspB. Ref.8

Secondary structure

..................... 109
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9EYW6 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: A4D002333A614362

FASTA10912,882
        10         20         30         40         50         60 
MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT 

        70         80         90        100 
AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV 

« Hide

References

« Hide 'large scale' references
[1]"Description of Staphylococcus serine protease (ssp) operon in Staphylococcus aureus and nonpolar inactivation of sspA-encoded serine protease."
Rice K., Peralta R., Bast D., de Azavedo J., McGavin M.J.
Infect. Immun. 69:159-169(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The Staphylococcus aureus NCTC 8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
(In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.); Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C. (2006)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
[3]"Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases."
Rzychon M., Sabat A., Kosowska K., Potempa J., Dubin A.
Mol. Microbiol. 49:1051-1066(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-8, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH STAPHOPAIN B.
[4]"Interactive regulatory pathways control virulence determinant production and stability in response to environmental conditions in Staphylococcus aureus."
Lindsay J.A., Foster S.J.
Mol. Gen. Genet. 262:323-331(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: REGULATION.
[5]"Identification of a novel maturation mechanism and restricted substrate specificity for the sspB cysteine protease of Staphylococcus aureus."
Massimi I., Park E., Rice K., Mueller-Esterl W., Sauder D., McGavin M.J.
J. Biol. Chem. 277:41770-41777(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INHIBITION BY SSPA.
[6]"The role and regulation of the extracellular proteases of Staphylococcus aureus."
Shaw L., Golonka E., Potempa J., Foster S.J.
Microbiology 150:217-228(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[7]"Cytoplasmic control of premature activation of a secreted protease zymogen: deletion of staphostatin B (sspC) in Staphylococcus aureus 8325-4 yields a profound pleiotropic phenotype."
Shaw L.N., Golonka E., Szmyd G., Foster S.J., Travis J., Potempa J.
J. Bacteriol. 187:1751-1762(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"The staphostatin-staphopain complex: a forward binding inhibitor in complex with its target cysteine protease."
Filipek R., Rzychon M., Oleksy A., Gruca M., Dubin A., Potempa J., Bochtler M.
J. Biol. Chem. 278:40959-40966(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH STAPHOPAIN B, MUTAGENESIS OF GLY-98.
[9]"A comparison of staphostatin B with standard mechanism serine protease inhibitors."
Filipek R., Potempa J., Bochtler M.
J. Biol. Chem. 280:14669-14674(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH STAPHOPAIN B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF309515 Genomic DNA. Translation: AAG45845.1.
CP000253 Genomic DNA. Translation: ABD30111.1.
RefSeqYP_499539.1. NC_007795.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1PXVX-ray1.80C/D1-109[»]
1Y4HX-ray1.93C/D1-109[»]
ProteinModelPortalQ9EYW6.
SMRQ9EYW6. Positions 1-109.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING93061.SAOUHSC_00986.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD30111; ABD30111; SAOUHSC_00986.
GeneID3920387.
KEGGsao:SAOUHSC_00986.
PATRIC19579495. VBIStaAur99865_0906.

Phylogenomic databases

HOGENOMHOG000279964.
OMANTSHNQY.
OrthoDBEOG6ND0KS.

Enzyme and pathway databases

BioCycSAUR93061:GIWJ-952-MONOMER.

Family and domain databases

Gene3D2.40.310.10. 1 hit.
InterProIPR016085. Protease_inh_b-brl_dom.
IPR014728. Staphostatin_A/B.
IPR015113. Staphostatin_B.
[Graphical view]
PfamPF09023. Staphostatin_B. 1 hit.
[Graphical view]
SUPFAMSSF50882. SSF50882. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ9EYW6.

Entry information

Entry nameSSPC_STAA8
AccessionPrimary (citable) accession number: Q9EYW6
Secondary accession number(s): Q2FZL4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: March 1, 2001
Last modified: July 9, 2014
This is version 74 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