Reviewed, UniProtKB/Swiss-Prot Q5HH35 (SSPA_STAAC)

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:	SACOL1057

Organism

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

Taxonomic identifier

93062 [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	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_0000026884
	Chain	69 – 336	268	Glutamyl endopeptidase		PRO_0000026885
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 By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5HH35-1 [UniParc]. Last modified February 15, 2005. Version 1. Checksum: 8B0F7F0C7996AA3E	FASTA	336	36,313
	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 NPDNGDTNNS DNPDAA

References

[1]

"Insights on evolution of virulence and resistance from the complete genome analysis of an early methicillin-resistant Staphylococcus aureus strain and a biofilm-producing methicillin-resistant Staphylococcus epidermidis strain." Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J., Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J., Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H., Vamathevan J.J., Khouri H. , Utterback T.R., Lee C., Dimitrov G., Jiang L., Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E., Fraser C.M. J. Bacteriol. 187:2426-2438(2005) [PubMed: 15774886] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000046 Genomic DNA. Translation: AAW36522.1.
RefSeq	YP_185922.1.
3D structure databases
SMR	Q5HH35. Positions 69-284.
ModBase	Search...
Protein-protein interaction databases
STRING	Q5HH35.
Genome annotation databases
GeneID	3237584.
GenomeReviews	Gene locus SACOL1057 in contig CP000046_GR.
KEGG	sac:SACOL1057.
TIGR	SACOL1057.
Phylogenomic databases
eggNOG	COG3591.
HOGENOM	HBG693141.
OMA	EDINFAN.
Enzyme and pathway databases
BioCyc	SAUR93062:SACOL1057-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_STAAC

Accession

Primary (citable) accession number: Q5HH35

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	February 15, 2005
Last modified:	January 19, 2010
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)