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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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Protease inhibitor, Thiol protease inhibitor

Keywords - Biological processi

Virulence

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 lineageiBacteriaFirmicutesBacilliBacillalesStaphylococcaceaeStaphylococcus
Proteomesi
  • UP000008816 Componenti: Chromosome

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi98G → A or R: Loss of affinity for SspB. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002205531 – 109Staphostatin BAdd BLAST109

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

1109
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 10Combined sources8
Helixi13 – 15Combined sources3
Helixi18 – 25Combined sources8
Beta strandi29 – 33Combined sources5
Turni34 – 37Combined sources4
Beta strandi38 – 44Combined sources7
Beta strandi50 – 59Combined sources10
Turni60 – 63Combined sources4
Beta strandi64 – 69Combined sources6
Beta strandi72 – 83Combined sources12
Beta strandi86 – 97Combined sources12
Beta strandi103 – 107Combined sources5

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiQ9EYW6.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni97 – 101Binds to staphopain B5

Sequence similaritiesi

Phylogenomic databases

HOGENOMiHOG000279964.
OMAiNTSHNQY.

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:March 1, 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.
RefSeqiWP_000284457.1. NC_007795.1.
YP_499539.1. NC_007795.1.

Genome annotation databases

EnsemblBacteriaiABD30111; ABD30111; SAOUHSC_00986.
GeneIDi28381407.
3920387.
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.
RefSeqiWP_000284457.1. NC_007795.1.
YP_499539.1. NC_007795.1.

3D structure databases

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

Protein-protein interaction databases

STRINGi93061.SAOUHSC_00986.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD30111; ABD30111; SAOUHSC_00986.
GeneIDi28381407.
3920387.
KEGGisao:SAOUHSC_00986.
PATRICi19579495. VBIStaAur99865_0906.

Phylogenomic databases

HOGENOMiHOG000279964.
OMAiNTSHNQY.

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...

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: November 2, 2016
This is version 86 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

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 one 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.