Reviewed, UniProtKB/Swiss-Prot Q8NX98 (SSPA_STAAW)

Names and origin

Protein names

Recommended name:
    Glutamyl endopeptidase
    EC=3.4.21.19
Alternative name(s):
    Staphylococcal serine proteinase
    V8 protease
    V8 proteinase
    Endoproteinase Glu-C

Gene names

Name:	sspA
Ordered Locus Names:	MW0932

Organism

Staphylococcus aureus (strain MW2) [Complete proteome] [HAMAP]

Taxonomic identifier

196620 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	327 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease sspB and inactivation of sspC, an inhibitor of sspB. It is the most important protease for degradation of fibronectin-binding protein (FnBP) and surface protein A, which are involved in adherence to host cells. May also protect bacteria against host defense mechanism by cleaving the immunoglobulin classes IgG, IgA and IgM. May be involved in the stability of secreted lipases By similarity.
Catalytic activity	Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
Subcellular location	Secreted By similarity.
Post-translational modification	Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA By similarity.
Miscellaneous	The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB By similarity.
Sequence similarities	Belongs to the peptidase S1B family.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Repeat Signal
Molecular function	Hydrolase Protease Serine protease
PTM	Zymogen
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	pathogenesis Inferred from electronic annotation. Source: UniProtKB-KW proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	serine-type endopeptidase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Potential
	Propeptide	30 – 68	39	By similarity		PRO_0000026894
	Chain	69 – 327	259	Glutamyl endopeptidase		PRO_0000026895
Regions
	Repeat	289 – 291	3	1
	Repeat	292 – 294	3	2
	Repeat	295 – 297	3	3
	Repeat	298 – 300	3	4
	Repeat	301 – 303	3	5
	Repeat	304 – 306	3	6
	Repeat	307 – 309	3	7
	Repeat	310 – 312	3	8
	Repeat	313 – 315	3	9
	Region	289 – 315	27	9 X 3 AA repeats of P-[DN]-N
Sites
	Active site	119	1	Charge relay system By similarity
	Active site	161	1	Charge relay system By similarity
	Active site	237	1	Charge relay system By similarity
	Site	68 – 69	2	Cleavage; by aureolysin By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q8NX98-1 [UniParc]. Last modified October 1, 2002. Version 1. Checksum: 3A26D9A138E65367	FASTA	327	35,319
	10 20 30 40 50 60 MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QSQSSKQQTP KIQKGGNLKP 70 80 90 100 110 120 LEQREHANVI LPNNDRHQIT DTTNGHYAPV TYIQVEAPTG TFIASGVVVG KDTLLTNKHV 130 140 150 160 170 180 VDATHGDPHA LKAFPSAINQ DNYPNGGFTA EQITKYSGEG DLAIVKFSPN EQNKHIGEVV 190 200 210 220 230 240 KPATMSNNAE TQVNQNITVT GYPGDKPVAT MWESKGKITY LKGEAMQYDL STTGGNSGSP 250 260 270 280 290 300 VFNEKNEVIG IHWGGVPNEF NGAVFINENV RNFLKQNIED IHFANDDQPN NPDNPDNPNN 310 320 PDNPNNPNNP DNPDNGDNNN SDNPDAA

References

[1]

"Genome and virulence determinants of high virulence community-acquired MRSA." Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K. Lancet 359:1819-1827(2002) [PubMed: 12044378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	BA000033 Genomic DNA. Translation: BAB94797.1.
RefSeq	NP_645749.1.
3D structure databases
SMR	Q8NX98. Positions 69-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q8NX98.
Genome annotation databases
GeneID	1003044.
GenomeReviews	Gene locus MW0932 in contig BA000033_GR.
KEGG	sam:MW0932.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG3591.
HOGENOM	HBG693141.
OMA	EDINFAN.
Enzyme and pathway databases
BioCyc	SAUR196620:MW0932-MONOMER.
Family and domain databases
InterPro	IPR000126. Pept_S1B_AS. IPR001254. Peptidase_S1_S6. IPR008256. Peptidase_S1B. IPR008353. Peptidase_S1B_tx. IPR009003. Ser/Cys_Pept_Trypsin-like. [Graphical view]
Pfam	PF00089. Trypsin. 1 hit. [Graphical view]
PRINTS	PR01774. EXFOLTOXIN. PR00839. V8PROTEASE.
SMART	SM00020. Tryp_SPc. 1 hit. [Graphical view]
PROSITE	PS00672. V8_HIS. 1 hit. PS00673. V8_SER. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

SSPA_STAAW

Accession

Primary (citable) accession number: Q8NX98

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	October 1, 2002
Last modified:	January 19, 2010
This is version 48 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)