Reviewed, UniProtKB/Swiss-Prot P81297 (SSPP_STAAU)

Names and origin

Protein names

Recommended name:
    Staphopain A
    EC=3.4.22.48
Alternative name(s):
    Staphylopain A
    Staphylococcal cysteine proteinase A

Gene names

Name:	sspP
Synonyms:	scpA

Organism

Staphylococcus aureus

Taxonomic identifier

1280 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length	388 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	Cysteine protease able to degrade elastin. Ref.3
Catalytic activity	Broad endopeptidase action on proteins including elastin, but rather limited hydrolysis of small-molecule substrates. Assays are conveniently made with hemoglobin, casein or Z-Phe-Arg-NHMec as substrate.
Enzyme regulation	Prematurely activated/folded staphopain A is inhibited by staphostatin A (scpB), which is probably required to protect staphylococcal cytoplasmic proteins from degradation by scpA. Also inactivated by heavy metal ions such as Hg2+ or Ag+, iodoacetamide, E-64 and human plasma. Ref.3
Subunit structure	In the cytoplasm, prematurely activated/folded scpA forms a stable non-covalent complex with scpB.
Subcellular location	Secreted.
Induction	Expression occurs in a growth phase-dependent manner with optimal expression at post-exponential phase. Up-regulated by agr (accessory gene regulator) and repressed by sarA (staphylococcal accessory regulator) and sigmaB factor.
Post-translational modification	Cleavage leads to the activation of scpA probably by an auto-catalytic manner.
Miscellaneous	The catalytic maturation of scpA appears to reside outside the cascade of activation started by the metalloprotease aureolysin (aur).
Sequence similarities	Belongs to the peptidase C47 family.
biophysicochemical properties	Kinetic parameters: KM=0.5 mM for CBZ-Phe-Leu-Glu-pNA pH dependence: Optimum pH is 6.5 for elastin hydrolysis.

Ontologies

Keywords
Biological process	Virulence
Cellular component	Secreted
Domain	Signal
Molecular function	Hydrolase Protease Thiol 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	cysteine-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 – 25

25

Potential

Propeptide

26 – 214

189

Ref.2

PRO_0000026545

Chain

215 – 388

174

Staphopain A

PRO_0000026546

Sites

Active site

238

1

By similarity

Active site

334

1

By similarity

Active site

355

1

By similarity

Site

214 – 215

2

Cleavage

Experimental info

Sequence conflict

288

1

E → G AA sequence Ref.2

Secondary structure

1

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388

Helix Strand Turn

Details...

Beta strand

217 – 222

6

Beta strand

234 – 236

3

Helix

238 – 251

14

Helix

258 – 265

8

Helix

271 – 276

6

Helix

281 – 290

10

Beta strand

296 – 300

5

Helix

304 – 312

9

Beta strand

317 – 325

9

Beta strand

333 – 344

12

Beta strand

349 – 354

6

Beta strand

362 – 365

4

Beta strand

370 – 372

3

Beta strand

378 – 386

9

Sequences

	Sequence		Length	Mass (Da)
	P81297-1 [UniParc]. Last modified July 5, 2005. Version 2. Checksum: 6E29DE8D0D7DFC42	FASTA	388	44,120
	10 20 30 40 50 60 MKRNFPKLIA LSLIFSLSIT PIANAESNSN IKAKDKRHVQ VNVEDKSVPT DVRNLAQKDY 70 80 90 100 110 120 LSYVTSLDKI YNKEKASYTL GEPFKIYKFN KKSDGNYYFP VLNTEGNIDY IVTISPKVTK 130 140 150 160 170 180 DSSSSSKYTI NVSSFLSKAL NEYKDQQITI LTNSKGYYVV TQNHKAKLVL KTPRLEDKKA 190 200 210 220 230 240 KKTESIPTGN NVTQLKQKAS VTMPTSQFKS NNYTYNEQYV NKLENFKIRE TQGNNGWCAG 250 260 270 280 290 300 YTMSALLNAT YNTNKYHAEA VMRFLHPNLQ GQQFQFTGLT PREMIYFEQT QGRSPQLLNR 310 320 330 340 350 360 MTTYNEVDNL TKNNKGIAIL GSRVESRNGM HAGHAMAVVG NAKLNNGQEV IIIWNPWDNG 370 380 FMTQDAKNNV IPVSNGDHYQ WYSSIYGY

References

[1]	"Genetic characterization of staphopain genes in Staphylococcus aureus." Golonka E., Filipek R., Sabat A., Sinczak A., Potempa J. Biol. Chem. 385:1059-1067(2004) [PubMed: 15576326] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 27733 / V8.
[2]	Kiess M., Hofmann B., Weissflog S., Schomburg D. Submitted (APR-1998) to UniProtKB Cited for: PROTEIN SEQUENCE OF 215-388. Strain: ATCC 27733 / V8.
[3]	"Degradation of elastin by a cysteine proteinase from Staphylococcus aureus." Potempa J., Dubin A., Korzus G., Travis J. J. Biol. Chem. 263:2664-2667(1988) [PubMed: 3422637] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: ATCC 27733 / V8.
[4]	"A novel class of cysteine protease inhibitors: solution structure of staphostatin A from Staphylococcus aureus." Dubin G., Krajewski M., Popowicz G., Stec-Niemczyk J., Bochtler M., Potempa J., Dubin A., Holak T.A. Biochemistry 42:13449-13456(2003) [PubMed: 14621990] [Abstract] Cited for: INTERACTION WITH STAPHOSTATIN A. Strain: ATCC 27733 / V8.
[5]	"Staphostatins: an expanding new group of proteinase inhibitors with a unique specificity for the regulation of staphopains, Staphylococcus spp. cysteine proteinases." Rzychon M., Sabat A., Kosowska K., Potempa J., Dubin A. Mol. Microbiol. 49:1051-1066(2003) [PubMed: 12890028] [Abstract] Cited for: INTERACTION WITH STAPHOSTATIN A. Strain: ATCC 27733 / V8.
[6]	"Crystal structure of a thiol proteinase from Staphylococcus aureus V-8 in the E-64 inhibitor complex." Hofmann B., Schomburg D., Hecht H.-J. Acta Crystallogr. A 49:102-102(1993) Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 215-388 IN COMPLEX WITH E-64. Strain: ATCC 27733 / V8.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AJ538362 Genomic DNA. Translation: CAD61962.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CV8	X-ray	1.75	A	215-388	[»]

ModBase

Search...

Enzyme and pathway databases

BRENDA

3.4.22.48. 95.

Family and domain databases

InterPro

IPR000169. Pept_cys_AS.
IPR008750. Peptidase_C47.
[Graphical view]

Pfam

PF05543. Peptidase_C47. 1 hit.
[Graphical view]

PROSITE

PS00640. THIOL_PROTEASE_ASN. False negative.
PS00139. THIOL_PROTEASE_CYS. False negative.
PS00639. THIOL_PROTEASE_HIS. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

SSPP_STAAU

Accession

Primary (citable) accession number: P81297
Secondary accession number(s): Q70UR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	July 5, 2005
Last modified:	June 16, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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