NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1016/S0140-6736(02)08713-5; PubMed=12044378 [NCBI, ExPASy, EBI, Israel, Japan]
Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y., Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
"Genome and virulence determinants of high virulence community-acquired MRSA.";
Lancet 359:1819-1827(2002).

Comments

FUNCTION: Cysteine protease able to degrade elastin (By similarity).
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 (By similarity).
SUBUNIT: In the cytoplasm, prematurely activated/folded scpA forms a stable non-covalent complex with scpB (By similarity).
SUBCELLULAR LOCATION: Secreted (By similarity).
PTM: Cleavage leads to the activation of scpA probably by an auto-catalytic manner (By similarity).
MISCELLANEOUS: The catalytic maturation of scpA appears to reside outside the cascade of activation started by the metalloprotease aureolysin (aur) (By similarity).
SIMILARITY: Belongs to the peptidase C47 family [view classification].

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

BA000033; BAB95715.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_646667.1; -.

3D structure databases

HSSP

P81297; 1CV8. [HSSP ENTRY / PDB]

SMR

Q8NVS9; 216-388.

ModBase

Q8NVS9.

Protein family/group databases

MEROPS

C47.001; -.

Enzyme and pathway databases

BioCyc

SAUR196620:MW1850-MON; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0004197;	Molecular function: cysteine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0009405;	Biological process: pathogenesis (inferred from electronic annotation from UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000169; Pept_cys_AS.
IPR008750; Peptidase_C47.
Graphical view of domain structure.

Pfam

PF05543; Peptidase_C47; 1.
Pfam graphical view of domain structure.

PROSITE

PS00640; THIOL_PROTEASE_ASN; FALSE_NEG.
PS00139; THIOL_PROTEASE_CYS; FALSE_NEG.
PS00639; THIOL_PROTEASE_HIS; 1.

ProtoNet

Q8NVS9.

Genome annotation databases

GeneID

1003965; -.

GenomeReviews

BA000033_GR; MW1850.

KEGG

sam:MW1850; -.

Phylogenomic databases

HOGENOM

Q8NVS9; -.

Genome annotation databases

CMR

Q8NVS9; MW1850.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; Protease; Secreted; Signal; Thiol protease; Virulence; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 25`	`25`	`Potential.`
`PROPEP`	`26 214`	`189`	`By similarity.`	`PRO_0000026557`
`CHAIN`	`215 388`	`174`	`Staphopain A.`	`PRO_0000026558`
`ACT_SITE`	`238 238`		`By similarity.`
`ACT_SITE`	`334 334`		`By similarity.`
`ACT_SITE`	`355 355`		`By similarity.`
`SITE`	`214 215`	`2`	`Cleavage (By similarity).`

Sequence information

Length: 388 AA [This is the length of the unprocessed precursor]

Molecular weight: 44142 Da [This is the MW of the unprocessed precursor]

CRC64: 0D502FD9F50933F7 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRNFPKLIA LSLILSLSVT PIANAESNSN IKAKDKKHVQ VNVEDKSIPT EVRNLAQKDY 

        70         80         90        100        110        120 
LSYVTSLDKI YNKEKASYTL GEPFKIYKFN KKSDGNYYFP VLNTEGNIDY IVTISPKVTK 

       130        140        150        160        170        180 
YSSSSSKYTI NVSPFLSKVL NQYKDQQITI LTNSKGYYVV TQNHKAKLVL KTPRLEDKKL 

       190        200        210        220        230        240 
KKTESIPTGN NVTQLKQKAS VTMPTSQFKS NNYTYNEQYV NKLENFKIRE TQGNNGWCAG 

       250        260        270        280        290        300 
YTMSALLNAT YNTNKYHAEA VMRFLHPNLQ GQRFQFTGLT PREMIYFGQT QGRSPQLLNR 

       310        320        330        340        350        360 
MTTYNEVDNL TKNNKGIAVL GSRVESRNGM HAGHAMAVVG NAKLDNGQEV IIIWNPWDNG 

       370        380 
FMTQDAKNNV IPVSNGDHYQ WYSSIYGY

Q8NVS9 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools