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Protein

Staphostatin B

Gene

sspC

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  1. cysteine-type endopeptidase inhibitor activity Source: UniProtKB-KW

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Keywords - Biological processi

Virulence

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-952-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Staphostatin B
Alternative name(s):
Staphylococcal cysteine protease B inhibitor
Gene namesi
Name:sspC
Ordered Locus Names:SAOUHSC_00986
OrganismiStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifieri93061 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcus
ProteomesiUP000008816 Componenti: Chromosome

Subcellular locationi

Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi98 – 981G → A or R: Loss of affinity for SspB. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 109109Staphostatin BPRO_0000220553Add
BLAST

Expressioni

Inductioni

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.1 Publication

Interactioni

Subunit structurei

Forms a stable non-covalent complex with prematurely activated/folded SspB.2 Publications

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00986.

Structurei

Secondary structure

1
109
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 108Combined sources
Helixi13 – 153Combined sources
Helixi18 – 258Combined sources
Beta strandi29 – 335Combined sources
Turni34 – 374Combined sources
Beta strandi38 – 447Combined sources
Beta strandi50 – 5910Combined sources
Turni60 – 634Combined sources
Beta strandi64 – 696Combined sources
Beta strandi72 – 8312Combined sources
Beta strandi86 – 9712Combined sources
Beta strandi103 – 1075Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PXVX-ray1.80C/D1-109[»]
1Y4HX-ray1.93C/D1-109[»]
ProteinModelPortaliQ9EYW6.
SMRiQ9EYW6. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9EYW6.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni97 – 1015Binds to staphopain B

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000279964.
OMAiNTSHNQY.
OrthoDBiEOG6ND0KS.

Family and domain databases

Gene3Di2.40.310.10. 1 hit.
InterProiIPR016085. Protease_inh_b-brl_dom.
IPR014728. Staphostatin_A/B.
IPR015113. Staphostatin_B.
[Graphical view]
PfamiPF09023. Staphostatin_B. 1 hit.
[Graphical view]
SUPFAMiSSF50882. SSF50882. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9EYW6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH
60 70 80 90 100
NQYHILFIDT AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS

RPIVYERLV
Length:109
Mass (Da):12,882
Last modified:February 28, 2001 - v1
Checksum:iA4D002333A614362
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309515 Genomic DNA. Translation: AAG45845.1.
CP000253 Genomic DNA. Translation: ABD30111.1.
RefSeqiYP_499539.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30111; ABD30111; SAOUHSC_00986.
GeneIDi3920387.
KEGGisao:SAOUHSC_00986.
PATRICi19579495. VBIStaAur99865_0906.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF309515 Genomic DNA. Translation: AAG45845.1.
CP000253 Genomic DNA. Translation: ABD30111.1.
RefSeqiYP_499539.1. NC_007795.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PXVX-ray1.80C/D1-109[»]
1Y4HX-ray1.93C/D1-109[»]
ProteinModelPortaliQ9EYW6.
SMRiQ9EYW6. Positions 1-109.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD30111; ABD30111; SAOUHSC_00986.
GeneIDi3920387.
KEGGisao:SAOUHSC_00986.
PATRICi19579495. VBIStaAur99865_0906.

Phylogenomic databases

HOGENOMiHOG000279964.
OMAiNTSHNQY.
OrthoDBiEOG6ND0KS.

Enzyme and pathway databases

BioCyciSAUR93061:GIWJ-952-MONOMER.

Miscellaneous databases

EvolutionaryTraceiQ9EYW6.

Family and domain databases

Gene3Di2.40.310.10. 1 hit.
InterProiIPR016085. Protease_inh_b-brl_dom.
IPR014728. Staphostatin_A/B.
IPR015113. Staphostatin_B.
[Graphical view]
PfamiPF09023. Staphostatin_B. 1 hit.
[Graphical view]
SUPFAMiSSF50882. SSF50882. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(2000) [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. (2005)
    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(2002) [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(1998) [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(2001) [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(2003) [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(2004) [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(2002) [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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH STAPHOPAIN B.

Entry informationi

Entry nameiSSPC_STAA8
AccessioniPrimary (citable) accession number: Q9EYW6
Secondary accession number(s): Q2FZL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 15, 2005
Last sequence update: February 28, 2001
Last modified: January 6, 2015
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.