NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0167-4781(92)90108-C; PubMed=1581352 [NCBI, ExPASy, EBI, Israel, Japan]
Narinx E., Davail S., Feller G., Gerday C.;
"Nucleotide and derived amino acid sequence of the subtilisin from the antarctic psychrotroph Bacillus TA39.";
Biochim. Biophys. Acta 1131:111-113(1992).

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 1 calcium ion per subunit (Potential).
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Still active at temperatures close to 0 degrees Celsius. Thermolabile;
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

X62369; CAA44227.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S23407; S23407.

3D structure databases

HSSP

Q9S3L6; 1EA7. [HSSP ENTRY / PDB]

SMR

P28842; 112-420.

ModBase

P28842.

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:0004252;	Molecular function: serine-type endopeptidase activity (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
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

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 26`	`26`	`Potential.`
`PROPEP`	`27 111`	`85`	`Potential.`	`PRO_0000027181`
`CHAIN`	`112 420`	`309`	`Subtilisin.`	`PRO_0000027182`
`ACT_SITE`	`145 145`		`Charge relay system (By similarity).`
`ACT_SITE`	`182 182`		`Charge relay system (By similarity).`
`ACT_SITE`	`360 360`		`Charge relay system (By similarity).`
`METAL`	`115 115`		`Calcium (Potential).`
`METAL`	`154 154`		`Calcium (Potential).`

Sequence information

Length: 420 AA [This is the length of the unprocessed precursor]

Molecular weight: 44087 Da [This is the MW of the unprocessed precursor]

CRC64: AE4F121BD32B26EC [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKRSGKIFTT AMLAVTLMMP AMGVSANEGN AAAEGNEKFR VLVDSVDQKN LKNAKQQYGV 

        70         80         90        100        110        120 
HWDFAGEGFT TDMNEKQFNA LKKNKNLTVE KVPELEIATA TDKPEALYNA MAASQSTPWG 

       130        140        150        160        170        180 
IKAIYNNSSI TQTSGGGGIN IAVLDTGVNT NHPDLRNNVE QCKDFTVGTT YTNNSCTDRQ 

       190        200        210        220        230        240 
GHGTHVAGSA LADGGTGNGV YGVAPDADLW AYKVLGDDGS GYADDIAAAI RHAGDQATAL 

       250        260        270        280        290        300 
NTKVVINMSL GSSGESSLIT NAVNYSYNKG VLIIAAAGNS GPYQGSIGYP GALVNAVAVA 

       310        320        330        340        350        360 
ALENKVENGT YRVADFSSRG YSWTDGDYAI QKGDVEISAP GAAIYSTWFD GGYATISGTS 

       370        380        390        400        410        420 
MASPHAAGLA AKIWAQYPSA SNVDVRGELQ YRAYENDILS GYYAGYGDDF ASGFGFATVQ

P28842 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