[1]	PROTEIN SEQUENCE. STRAIN=DY; PubMed=6420308 [NCBI, ExPASy, EBI, Israel, Japan] Nedkov P., Oberthur W., Braunitzer G.; "Primary structure of subtilisin DY."; Hoppe-Seyler's Z. Physiol. Chem. 364:1537-1540(1983).
[2]	X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS). STRAIN=DY; PubMed=9826175 [NCBI, ExPASy, EBI, Israel, Japan] Eschenburg S., Genov N., Peters K., Fittkau S., Stoeva S., Wilson K.S., Betzel C.; "Crystal structure of subtilisin DY, a random mutant of subtilisin Carlsberg."; Eur. J. Biochem. 257:309-318(1998).

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

3D structure databases

PDB

1BH6; X-ray; 1.75 A; A=1-274.

[ExPASy / RCSB / EBI]

PDBsum

1BH6; -.

ModBase

P00781.

Protein family/group databases

MEROPS

S08.037; -.

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

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`	`1 274`	`274`	`Subtilisin DY.`	`PRO_0000076417`
`ACT_SITE`	`32 32`		`Charge relay system.`
`ACT_SITE`	`63 63`		`Charge relay system.`
`ACT_SITE`	`220 220`		`Charge relay system.`
`METAL`	`2 2`		`Calcium 1.`
`METAL`	`41 41`		`Calcium 1.`
`METAL`	`74 74`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`76 76`		`Calcium 1.`
`METAL`	`80 80`		`Calcium 1; via carbonyl oxygen.`
`METAL`	`168 168`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`170 170`		`Calcium 2; via carbonyl oxygen.`
`METAL`	`173 173`		`Calcium 2; via carbonyl oxygen.`
`HELIX`	`7 10`	`4`
`HELIX`	`13 18`	`6`
`STRAND`	`27 33`	`7`
`STRAND`	`44 49`	`6`
`STRAND`	`60 62`	`3`
`HELIX`	`63 72`	`10`
`STRAND`	`75 79`	`5`
`STRAND`	`87 93`	`7`
`HELIX`	`103 115`	`13`
`STRAND`	`119 123`	`5`
`HELIX`	`132 143`	`12`
`STRAND`	`147 151`	`5`
`TURN`	`167 169`	`3`
`STRAND`	`173 179`	`7`
`STRAND`	`195 200`	`6`
`STRAND`	`202 208`	`7`
`TURN`	`209 211`	`3`
`STRAND`	`212 216`	`5`
`HELIX`	`219 236`	`18`
`HELIX`	`242 251`	`10`
`HELIX`	`259 262`	`4`
`HELIX`	`269 272`	`4`

Sequence information

Length: 274 AA [This is the length of the unprocessed precursor]

Molecular weight: 27436 Da [This is the MW of the unprocessed precursor]

CRC64: 0154696E22F46533 [This is a checksum on the sequence]

        10         20         30         40         50         60 
AQTVPYGIPL IKADKVQAQG YKGANVKVGI IDTGIAASHT DLKVVGGASF VSGESYNTDG 

        70         80         90        100        110        120 
NGHGTHVAGT VAALDNTTGV LGVAPNVSLY AIKVLNSSGS GTYSAIVSGI EWATQNGLDV 

       130        140        150        160        170        180 
INMSLGGPSG STALKQAVDK AYASGIVVVA AAGNSGSSGS QNTIGYPAKY DSVIAVGAVD 

       190        200        210        220        230        240 
SNKNRASFSS VGAELEVMAP GVSVYSTYPS NTYTSLNGTS MASPHVAGAA ALILSKYPTL 

       250        260        270 
SASQVRNRLS STATNLGDSF YYGKGLINVE AAAQ

P00781 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