Reviewed, UniProtKB/Swiss-Prot P0C1U8 (SSPA_STAAU)

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

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [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.3 Ref.4
Catalytic activity	Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
Subcellular location	Secreted. Ref.3
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	3D-structure 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.2

PRO_0000026882

Chain

69 – 336

268

Glutamyl endopeptidase

PRO_0000026883

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

Active site

161

1

Charge relay system

Active site

237

1

Charge relay system

Site

68 – 69

2

Cleavage; by aureolysin

Experimental info

Sequence conflict

109

1

Missing AA sequence Ref.2

Sequence conflict

125

1

Missing AA sequence Ref.2

Sequence conflict

145

1

N → D AA sequence Ref.2

Sequence conflict

193

1

V → T AA sequence Ref.2

Sequence conflict

229

1

D → N AA sequence Ref.2

Sequence conflict

259 – 261

3

EFN → QFD AA sequence Ref.2

Sequence conflict

268 – 270

3

ENV → NEVN AA sequence Ref.2

Secondary structure

1

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336

Helix Strand Turn

Details...

Beta strand

75 – 80

6

Helix

85 – 87

3

Beta strand

90 – 96

7

Beta strand

101 – 108

8

Beta strand

110 – 116

7

Helix

118 – 121

4

Helix

122 – 124

3

Helix

128 – 130

3

Beta strand

131 – 135

5

Beta strand

148 – 155

8

Beta strand

157 – 160

4

Beta strand

163 – 167

5

Helix

176 – 179

4

Beta strand

196 – 201

6

Beta strand

211 – 222

12

Beta strand

225 – 230

6

Beta strand

240 – 242

3

Beta strand

248 – 256

9

Turn

257 – 259

3

Beta strand

260 – 265

6

Helix

268 – 277

10

Sequences

	Sequence		Length	Mass (Da)
	P0C1U8-1 [UniParc]. Last modified September 5, 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

[1]	"Nucleotide sequence of the serine protease gene of Staphylococcus aureus, strain V8." Carmona C., Gray G.L. Nucleic Acids Res. 15:6757-6757(1987) [PubMed: 3306605] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27733 / V8.
[2]	"The primary structure of staphylococcal protease." Drapeau G.R. Can. J. Biochem. 56:534-544(1978) [PubMed: 96922] [Abstract] Cited for: PROTEIN SEQUENCE OF 69-280. Strain: ATCC 27733 / V8.
[3]	"Purification and properties of an extracellular protease of Staphylococcus aureus." Drapeau G.R., Boily Y., Houmard J. J. Biol. Chem. 247:6720-6726(1972) [PubMed: 4627743] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION. Strain: ATCC 27733 / V8.
[4]	"Cleavage of human immunoglobulins by serine proteinase from Staphylococcus aureus." Prokesova L., Potuznikova B., Potempa J., Zikan J., Radl J., Hachova L., Baran K., Porwit-Bobr Z., John C. Immunol. Lett. 31:259-265(1992) [PubMed: 1372285] [Abstract] Cited for: FUNCTION. Strain: ATCC 27733 / V8.
[5]	"Crystal structure of an alkaline form of V8 protease from Staphylococcus aureus." Yamada K., Ohta M., Hasegawa T., Torii K., Murakami M., Kouyama K. Submitted (JUN-2004) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 69-336. Strain: ATCC 27733 / V8.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBLGenBankDDBJ

Y00356 Genomic DNA. Translation: CAA68434.1.

PIR

PRSASK. A26812.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1WCZ	X-ray	2.00	A	69-336	[»]

ModBase

Search...

Protein family/group databases

MEROPS

S01.269.

Enzyme and pathway databases

BRENDA

3.4.21.19. 95.

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_STAAU

Accession

Primary (citable) accession number: P0C1U8
Secondary accession number(s): P04188

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 5, 2006
Last sequence update:	September 5, 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)