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Q9EYW6

- SSPC_STAA8

UniProt

Q9EYW6 - SSPC_STAA8

Protein

Staphostatin B

Gene

sspC

Organism
Staphylococcus aureus (strain NCTC 8325)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. 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

    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: Chromosome

    Subcellular locationi

    Cytoplasm 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    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 – 108
    Helixi13 – 153
    Helixi18 – 258
    Beta strandi29 – 335
    Turni34 – 374
    Beta strandi38 – 447
    Beta strandi50 – 5910
    Turni60 – 634
    Beta strandi64 – 696
    Beta strandi72 – 8312
    Beta strandi86 – 9712
    Beta strandi103 – 1075

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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

    MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH    50
    NQYHILFIDT AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS 100
    RPIVYERLV 109
    Length:109
    Mass (Da):12,882
    Last modified:March 1, 2001 - v1
    Checksum:iA4D002333A614362
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309515 Genomic DNA. Translation: AAG45845.1.
    CP000253 Genomic DNA. Translation: ABD30111.1.
    RefSeqiWP_000284457.1. NC_007795.1.
    YP_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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF309515 Genomic DNA. Translation: AAG45845.1 .
    CP000253 Genomic DNA. Translation: ABD30111.1 .
    RefSeqi WP_000284457.1. NC_007795.1.
    YP_499539.1. NC_007795.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1PXV X-ray 1.80 C/D 1-109 [» ]
    1Y4H X-ray 1.93 C/D 1-109 [» ]
    ProteinModelPortali Q9EYW6.
    SMRi Q9EYW6. Positions 1-109.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 93061.SAOUHSC_00986.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ABD30111 ; ABD30111 ; SAOUHSC_00986 .
    GeneIDi 3920387.
    KEGGi sao:SAOUHSC_00986.
    PATRICi 19579495. VBIStaAur99865_0906.

    Phylogenomic databases

    HOGENOMi HOG000279964.
    OMAi NTSHNQY.
    OrthoDBi EOG6ND0KS.

    Enzyme and pathway databases

    BioCyci SAUR93061:GIWJ-952-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q9EYW6.

    Family and domain databases

    Gene3Di 2.40.310.10. 1 hit.
    InterProi IPR016085. Protease_inh_b-brl_dom.
    IPR014728. Staphostatin_A/B.
    IPR015113. Staphostatin_B.
    [Graphical view ]
    Pfami PF09023. Staphostatin_B. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50882. SSF50882. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiSSPC_STAA8
    AccessioniPrimary (citable) accession number: Q9EYW6
    Secondary accession number(s): Q2FZL4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 16, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 76 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