[1]	PROTEIN SEQUENCE. Svendsen I., Genov N., Idakieva K.; "Complete amino acid sequence of alkaline mesentericopeptidase: a subtilisin isolated from a strain of Bacillus mesentericus."; FEBS Lett. 196:228-232(1986).
[2]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). DOI=10.1107/S0108768191004202; PubMed=1793542 [NCBI, ExPASy, EBI, Israel, Japan] Dauter Z., Betzel C., Genov N., Pipon N., Wilson K.S.; "Complex between the subtilisin from a mesophilic bacterium and the leech inhibitor eglin-C."; Acta Crystallogr. B 47:707-730(1991).

Comments

FUNCTION: Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
CATALYTIC ACTIVITY: Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
COFACTOR: Binds 2 calcium ions per subunit.
SUBCELLULAR LOCATION: Secreted.
MISCELLANEOUS: Secretion of subtilisin is associated with onset of sporulation, and many mutations which block sporulation at early stages affect expression levels of subtilisin. However, subtilisin is not necessary for normal sporulation.
SIMILARITY: Belongs to the peptidase S8 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

PIR

A23624; A23624.

3D structure databases

PDB

1MEE; X-ray; 2.00 A; A=1-275.

[ExPASy / RCSB / EBI]

PDBsum

1MEE; -.

ModBase

P07518.

Protein family/group databases

MEROPS

S08.002; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-KW).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030435;	Biological process: sporulation resulting in formation of a cellular spore (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR000209; Pept_S8_S53.
IPR015500; Peptidase_S8_subtilisin-rel.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.200; Pept_S8_S53; 1.

PANTHER

PTHR10795; SubtilSerProt; 1.

Pfam

PF00082; Peptidase_S8; 1.
Pfam graphical view of domain structure.

PRINTS

PR00723; SUBTILISIN.

PROSITE

PS00136; SUBTILASE_ASP; 1.
PS00137; SUBTILASE_HIS; 1.
PS00138; SUBTILASE_SER; 1.

Other

P07518; -.

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

Keywords

3D-structure; Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease; Sporulation.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 275`	`275`	`Subtilisin.`	`PRO_0000076419`
`ACT_SITE`	`32 32`		`By similarity.`
`ACT_SITE`	`64 64`		`By similarity.`
`ACT_SITE`	`221 221`		`By similarity.`
`METAL`	`2 2`		`Calcium 1.`
`METAL`	`41 41`		`Calcium 1.`
`METAL`	`75 75`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`77 77`		`Calcium 1.`
`METAL`	`79 79`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`81 81`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`169 169`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`171 171`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`174 174`		`Calcium 2; via carbonyl oxygen.`
`HELIX`	`6 10`	`5`
`HELIX`	`13 19`	`7`
`STRAND`	`27 33`	`7`
`STRAND`	`44 49`	`6`
`HELIX`	`65 73`	`9`
`STRAND`	`76 80`	`5`
`STRAND`	`88 94`	`7`
`HELIX`	`104 116`	`13`
`STRAND`	`120 124`	`5`
`STRAND`	`126 130`	`5`
`HELIX`	`133 144`	`12`
`STRAND`	`148 152`	`5`
`TURN`	`168 170`	`3`
`STRAND`	`174 180`	`7`
`STRAND`	`198 201`	`4`
`STRAND`	`203 209`	`7`
`TURN`	`210 212`	`3`
`STRAND`	`213 217`	`5`
`HELIX`	`220 237`	`18`
`HELIX`	`243 252`	`10`
`HELIX`	`260 263`	`4`
`HELIX`	`270 273`	`4`

Sequence information

Length: 275 AA [This is the length of the unprocessed precursor]

Molecular weight: 27656 Da [This is the MW of the unprocessed precursor]

CRC64: 33BDA897DBA4170A [This is a checksum on the sequence]

        10         20         30         40         50         60 
AQSVPYGISQ IKAPALHSQG YTGSNVKVAV IDSGIDSSHP DLNVRGGASF VPSETNPYQD 

        70         80         90        100        110        120 
GSSHGTHVAG TIAALNNSIG VLGVAPSSAL YAVKVLDSTG SGQYSWIING IEWAISNNMD 

       130        140        150        160        170        180 
VINMSLGGPT GSTALKTVVD KAVSSGIVVA AAAGNEGSSG STSTVGYPAK YPSTIAVGAV 

       190        200        210        220        230        240 
NSANQRASFS SAGSELDVMA PGVSIQSTLP GGTYGAYNGT SMATPHVAGA AALILSKHPT 

       250        260        270 
WTNAQVRDRL ESTATYLGSS FYYGKGLINV QAAAQ

P07518 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