Q9EYW6 (SSPC_STAA8) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Staphostatin B

Alternative name(s):
Staphylococcal cysteine protease B inhibitor

Gene names

Name:	sspC
Ordered Locus Names:	SAOUHSC_00986

Organism

Staphylococcus aureus (strain NCTC 8325) [Reference proteome] [HAMAP]

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Firmicutes › Bacilli › Bacillales › Staphylococcaceae › Staphylococcus › Staphylococcus aureus › Staphylococcus aureus subsp. aureus

Protein attributes

Sequence length	109 AA.
Sequence status	Complete.
Protein existence	Evidence 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 process	Virulence
Cellular component	Cytoplasm
Molecular function	Protease inhibitor Thiol protease inhibitor
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of endopeptidase activity Inferred from electronic annotation. Source: GOC pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	cysteine-type endopeptidase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 109

109

Staphostatin B

PRO_0000220553

Regions

Region

97 – 101

5

Binds to staphopain B

Experimental info

Mutagenesis

98

1

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

Secondary structure

1

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109

Helix Strand Turn

Details...

Beta strand

3 – 10

8

Helix

13 – 15

3

Helix

18 – 25

8

Beta strand

29 – 33

5

Turn

34 – 37

4

Beta strand

38 – 44

7

Beta strand

50 – 59

10

Turn

60 – 63

4

Beta strand

64 – 69

6

Beta strand

72 – 83

12

Beta strand

86 – 97

12

Beta strand

103 – 107

5

Sequences

	Sequence		Length	Mass (Da)
	Q9EYW6 [UniParc]. Last modified March 1, 2001. Version 1. Checksum: A4D002333A614362	FASTA	109	12,882
	10 20 30 40 50 60 MYQLQFINLV YDTTKLTHLE QTNINLFIGN WSNHQLQKSI CIRHGDDTSH NQYHILFIDT 70 80 90 100 AHQRIKFSSI DNEEIIYILD YDDTQHILMQ TSSKQGIGTS RPIVYERLV

References

	« Hide 'large scale' referencesShow '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 NCTC8325 genome." Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J. Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases 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.

RefSeq

YP_499539.1. NC_007795.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q9EYW6.

SMR

Q9EYW6. Positions 1-109.

ModBase

Search...

Protein-protein interaction databases

STRING

93061.SAOUHSC_00986.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

ABD30111; ABD30111; SAOUHSC_00986.

GeneID

3920387.

KEGG

sao:SAOUHSC_00986.

PATRIC

19579495. VBIStaAur99865_0906.

Phylogenomic databases

HOGENOM

HOG000279964.

OMA

NTSHNQY.

ProtClustDB

CLSK885097.

Enzyme and pathway databases

BioCyc

SAUR93061:GIWJ-952-MONOMER.

Family and domain databases

Gene3D

2.40.310.10. 1 hit.

InterPro

IPR014728. Prot_inh_staphostatin.
IPR016085. Protease_inh_b-brl_dom.
IPR015113. Staphostatin_B.
[Graphical view]

Pfam

PF09023. Staphostatin_B. 1 hit.
[Graphical view]

SUPFAM

SSF50882. Protease_inh_b-brl. 1 hit.

ProtoNet

Search...

Other

EvolutionaryTrace

Q9EYW6.

Entry information

Entry name

SSPC_STAA8

Accession

Primary (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:	May 1, 2013
This is version 69 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program