Reviewed, UniProtKB/Swiss-Prot Q7A6A6 (SSPA_STAAN)

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:	SA0901

Organism

Staphylococcus aureus (strain N315) [Complete proteome] [HAMAP]

Taxonomic identifier

158879 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	342 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_0000026888
	Chain	69 – 342	274	Glutamyl endopeptidase		PRO_0000026889
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	316 – 318	3	9
	Repeat	319 – 321	3	10
	Repeat	322 – 324	3	11
	Repeat	325 – 327	3	12
	Repeat	328 – 330	3	13
	Region	289 – 330	42	13 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)
	Q7A6A6-1 [UniParc]. Last modified July 5, 2004. Version 1. Checksum: 5AEF42DCE01C4B24	FASTA	342	36,977
	10 20 30 40 50 60 MKGKFLKVSS LFVATLTTAT LVSSPAANAL SSKAMDNHPQ QTQSSKQQTP KIKKGGNLKP 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 310 320 330 340 PDNPNNPDNP NNPDEPNNPD NPNNPDNPDN GDNNNSDNPD AA

References

[1]

"Whole genome sequencing of meticillin-resistant Staphylococcus aureus." Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L., Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M., Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y. , Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H., Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K., Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H., Hiramatsu K. Lancet 357:1225-1240(2001) [PubMed: 11418146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	BA000018 Genomic DNA. Translation: BAB42146.1.
PIR	G89873.
RefSeq	NP_374168.1.
3D structure databases
SMR	Q7A6A6. Positions 69-284.
ModBase	Search...
Genome annotation databases
GeneID	1123724.
GenomeReviews	Gene locus SA0901 in contig BA000018_GR.
KEGG	sau:SA0901.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q7A6A6.
OMA	Q7A6A6. EDINFAN.
Enzyme and pathway databases
BioCyc	SAUR158879:SA0901-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_STAAN

Accession

Primary (citable) accession number: Q7A6A6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	July 5, 2004
Last modified:	June 16, 2009
This is version 35 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)