[1]	PROTEIN SEQUENCE. STRAIN=76; DOI=10.1021/bi00454a029; PubMed=2302386 [NCBI, ExPASy, EBI, Israel, Japan] Stoeva S., Kleinschmidt T., Mesrob B., Braunitzer G.; "Primary structure of a zinc protease from Bacillus mesentericus strain 76."; Biochemistry 29:527-534(1990).

Comments

FUNCTION: Extracellular zinc metalloprotease.
CATALYTIC ACTIVITY: Similar, but not identical, to that of thermolysin.
COFACTOR: Binds 4 calcium ions per subunit (Potential).
COFACTOR: Binds 1 zinc ion per subunit (Potential).
BIOPHYSICOCHEMICAL PROPERTIES:

Temperature dependence: Thermolabile;
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peptidase M4 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

HSSP

P81177; 1BQB. [HSSP ENTRY / PDB]

ModBase

P68734.

Protein family/group databases

MEROPS

M04.014; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0005509;	Molecular function: calcium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004222;	Molecular function: metalloendopeptidase activity (inferred from electronic annotation from InterPro).
GO:0008270;	Molecular function: zinc ion binding (inferred from electronic annotation from InterPro).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR006025; Pept_M_Zn_BS.
IPR013856; Peptidase_M4.
IPR001570; Peptidase_M4_C.
Graphical view of domain structure.

Gene3D

G3DSA:3.10.170.10; Peptidase_M4; 1.
G3DSA:1.10.390.10; Peptidase_M4/M36; 1.

Pfam

PF01447; Peptidase_M4; 1.
PF02868; Peptidase_M4_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00730; THERMOLYSIN.

PROSITE

PS00142; ZINC_PROTEASE; 1.

ProtoNet

P68734.

Other

UniRef

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

Keywords

Calcium; Direct protein sequencing; Hydrolase; Metal-binding; Metalloprotease; Protease; Secreted; Zinc.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 300`	`300`	`Bacillolysin.`	`PRO_0000078173`
`ACT_SITE`	`144 144`		`By similarity.`
`ACT_SITE`	`228 228`		`Proton donor (By similarity).`
`METAL`	`139 139`		`Calcium 1 (Potential).`
`METAL`	`143 143`		`Zinc; catalytic (By similarity).`
`METAL`	`147 147`		`Zinc; catalytic (By similarity).`
`METAL`	`167 167`		`Zinc; catalytic (By similarity).`
`METAL`	`178 178`		`Calcium 1 (Potential).`
`METAL`	`178 178`		`Calcium 2 (Potential).`
`METAL`	`181 181`		`Calcium 1 (Potential).`
`METAL`	`181 181`		`Calcium 2 (Potential).`
`METAL`	`183 183`		`Calcium 1; via carbonyl oxygen (Potential).`
`METAL`	`186 186`		`Calcium 1 (Potential).`
`METAL`	`186 186`		`Calcium 2 (Potential).`

Sequence information

Length: 300 AA [This is the length of the unprocessed precursor]

Molecular weight: 32674 Da [This is the MW of the unprocessed precursor]

CRC64: 6207B816C446385B [This is a checksum on the sequence]

        10         20         30         40         50         60 
AAATGSGTTL KGATVPLNIS YEGGKYVLRD LSKPTGTQII TYDLQNRQSR LPGTLVSSTT 

        70         80         90        100        110        120 
KTFTSSSQRA AVDAHYNLGK VYDYFYSNFK RNSYDNKGSK IVSSVHYGTQ YNNAAWTGDQ 

       130        140        150        160        170        180 
MIYGDGDGSF FSPLSGSLDV TAHEMTHGVT QETANLIYEN QPGALNESFS DVFGYFNDTE 

       190        200        210        220        230        240 
DWDIGEDITV SQPALRSLSN PTKYNQPDNY ANYRNLPNTD EGDYGGVHTN SGIPNKAAYN 

       250        260        270        280        290        300 
TITKLGVSKS QQIYYRALTT YLTPSSTFKD AKAALIQSAR DLYGSTDAAK VEAAWNAVGL

P68734 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