[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3139650 [NCBI, ExPASy, EBI, Israel, Japan] Yoshimoto T., Oyama H., Honda T., Tone H., Takeshita T., Kamiyama T., Tsuru D.; "Cloning and expression of subtilisin amylosacchariticus gene."; J. Biochem. 103:1060-1065(1988).
[2]	PARTIAL PROTEIN SEQUENCE. PubMed=4560201 [NCBI, ExPASy, EBI, Israel, Japan] Markland F.S., Kurihara M., Smith E.L.; "Subtilisin Amylosacchariticus. II. Isolation and sequence of the tryptic and cyanogen bromide peptides."; J. Biol. Chem. 247:5602-5618(1972).
[3]	PROTEIN SEQUENCE OF 107-381. PubMed=5055784 [NCBI, ExPASy, EBI, Israel, Japan] Kurihara M., Markland F.S., Smith E.L.; "Subtilisin Amylosacchariticus. 3. Isolation and sequence of the chymotryptic peptides and the complete amino acid sequence."; J. Biol. Chem. 247:5619-5631(1972).

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 (By similarity).
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

EMBL

D00264; BAA00186.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41448; SUBSS.

3D structure databases

HSSP

P04189; 1SCJ. [HSSP ENTRY / PDB]

SMR

P00783; 36-106, 107-381.

ModBase

P00783.

Protein family/group databases

MEROPS

I09.001; -.
S08.042; -.

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.
IPR010259; Prot_inh_S8A.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.50.200; Pept_S8_S53; 1.

PANTHER

PTHR10795; SubtilSerProt; 1.

Pfam

PF00082; Peptidase_S8; 1.
PF05922; Subtilisin_N; 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

Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Protease; Secreted; Serine protease; Signal; Sporulation; Zymogen.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 30`	`30`	`Potential.`
`PROPEP`	`31 106`	`76`	`Potential.`	`PRO_0000027183`
`CHAIN`	`107 381`	`275`	`Subtilisin amylosacchariticus.`	`PRO_0000027184`
`ACT_SITE`	`138 138`		`Charge relay system (By similarity).`
`ACT_SITE`	`170 170`		`Charge relay system (By similarity).`
`ACT_SITE`	`327 327`		`Charge relay system (By similarity).`
`METAL`	`108 108`		`Calcium 1 (By similarity).`
`METAL`	`147 147`		`Calcium 1 (By similarity).`
`METAL`	`181 181`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`183 183`		`Calcium 1 (By similarity).`
`METAL`	`185 185`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`187 187`		`Calcium 1; via carbonyl oxygen (By similarity).`
`METAL`	`275 275`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`277 277`		`Calcium 2; via carbonyl oxygen (By similarity).`
`METAL`	`280 280`		`Calcium 2; via carbonyl oxygen (By similarity).`
`CONFLICT`	`191 191`		`S -> A (in Ref. 2; AA sequence).`
`CONFLICT`	`365 365`		`N -> D (in Ref. 2; AA sequence).`

Sequence information

Length: 381 AA [This is the length of the unprocessed precursor]

Molecular weight: 39467 Da [This is the MW of the unprocessed precursor]

CRC64: 2251BADE22B4824F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MRSKKLWISL LFALTLIFTM AFSNMSAQAA GKSSTEKKYI VGFKQTMSAM SSAKKKDVIS 

        70         80         90        100        110        120 
EKGGKVQKQF KYVNAAAATL DEKAVKELKK DPSVAYVEED HIAHEYAQSV PYGISQIKAP 

       130        140        150        160        170        180 
ALHSQGYTGS NVKVAVIDSG IDSSHPDLNV RGGASFVPSE TNPYQDGSSH GTHVAGTIAA 

       190        200        210        220        230        240 
LNNSIGVLGV SPSASLYAVK VLDSTGSGQY SWIINGIEWA ISNNMDVINM SLGGPSGSTA 

       250        260        270        280        290        300 
LKTVVDKAVS SGIVVAAAAG NEGSSGSSST VGYPAKYPST IAVGAVNSSN QRASFSSAGS 

       310        320        330        340        350        360 
ELDVMAPGVS IQSTLPGGTY GAYNGTSMAT PHVAGAAALI LSKHPTWTNA QVRDRLESTA 

       370        380 
TYLGNSFYYG KGLINVQAAA Q

P00783 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