Reviewed, UniProtKB/Swiss-Prot Q2FZL2 (SSPA_STAA8)

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:	SAOUHSC_00988

Organism

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

Taxonomic identifier

93061 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	336 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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. Ref.1 Ref.3 Ref.5 Ref.7
Catalytic activity	Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
Subcellular location	Secreted By similarity.
Induction	Expression occurs in a growth-phase-dependent manner with optimal expression at post-exponential phase. Environmental conditions such as degree of aeration and salt concentration are also important in control of transcription and processing of sspA. Up-regulated by agr (accessory gene regulator) and repressed by sigmaB factor and sarA. Ref.3 Ref.6
Post-translational modification	Proteolytically cleaved by aureolysin (aur). This cleavage leads to the activation of sspA.
Miscellaneous	The cascade of activation of extracellular proteases proceeds from the metalloprotease aureolysin (aur), through sspA to sspB.
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 Direct protein sequencing
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	Ref.3		PRO_0000249327
	Chain	69 – 336	268	Glutamyl endopeptidase		PRO_0000249328
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	310 – 312	3	7
	Repeat	313 – 315	3	8
	Repeat	316 – 318	3	9
	Repeat	319 – 321	3	10
	Repeat	322 – 324	3	11
	Region	289 – 324	36	11 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

Sequences

	Sequence		Length	Mass (Da)
	Q2FZL2-1 [UniParc]. Last modified March 21, 2006. Version 1. Checksum: 8B138D0C7996AA3E	FASTA	336	36,326
	10 20 30 40 50 60 MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP 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 310 320 330 PDNPNNPDEP NNPDNPNNPD NPDNGDNNNS DNPDAA

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: 11119502] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[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].
[3]	"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: 14702415] [Abstract] Cited for: PROTEIN SEQUENCE OF 69-76, FUNCTION, INDUCTION.
[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: 10517329] [Abstract] Cited for: REGULATION.
[5]	"Decreased amounts of cell wall-associated protein A and fibronectin-binding proteins in Staphylococcus aureus sarA mutants due to up-regulation of extracellular proteases." Karlsson A., Saravia-Otten P., Tegmark K., Morfeldt E., Arvidson S. Infect. Immun. 69:4742-4748(2001) [PubMed: 11447146] [Abstract] Cited for: FUNCTION.
[6]	"Variation in extracellular protease production among clinical isolates of Staphylococcus aureus due to different levels of expression of the protease repressor sarA." Karlsson A., Arvidson S. Infect. Immun. 70:4239-4246(2002) [PubMed: 12117932] [Abstract] Cited for: INDUCTION.
[7]	"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: 12207024] [Abstract] Cited for: FUNCTION.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF309515 Genomic DNA. Translation: AAG45843.1. CP000253 Genomic DNA. Translation: ABD30113.1.
RefSeq	YP_499541.1.
3D structure databases
SMR	Q2FZL2. Positions 69-284.
ModBase	Search...
Genome annotation databases
GeneID	3920389.
GenomeReviews	Gene locus SAOUHSC_00988 in contig CP000253_GR.
KEGG	sao:SAOUHSC_00988.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q2FZL2.
OMA	Q2FZL2. EDINFAN.
Enzyme and pathway databases
BioCyc	SAUR93061:SAOUHSC_00988-MON.
Family and domain databases
InterPro	IPR000126. Pept_S1B_AS. IPR001254. Peptidase_S1_S6. IPR008256. Peptidase_S1B. IPR008353. Peptidase_S1B_tx. [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_STAA8

Accession

Primary (citable) accession number: Q2FZL2
Secondary accession number(s): P04188

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	March 21, 2006
Last modified:	June 16, 2009
This is version 23 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)