NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 287-301.
STRAIN=72;
PubMed=1834632 [NCBI, ExPASy, EBI, Israel, Japan]
Takekawa S., Uozumi N., Tsukagoshi N., Udaka S.;
"Proteases involved in generation of beta- and alpha-amylases from a large amylase precursor in Bacillus polymyxa.";
J. Bacteriol. 173:6820-6825(1991).

Comments

FUNCTION: Involved in the generation of beta- and alpha-amylases from the large amylase precursor.
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).
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

Sequence databases

EMBL

D00861; BAA00734.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A41335; A41335.

3D structure databases

HSSP

P05806; 1NPC. [HSSP ENTRY / PDB]

ModBase

P29148.

Protein family/group databases

MEROPS

M04.001; -.

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

IPR005075; Pept_M4_propep_PepSY.
IPR006025; Pept_M_Zn_BS.
IPR013856; Peptidase_M4.
IPR001570; Peptidase_M4_C.
IPR011096; Propep_M4_M36.
Graphical view of domain structure.

Gene3D

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

Pfam

PF07504; FTP; 1.
PF03413; PepSY; 1.
PF01447; Peptidase_M4; 1.
PF02868; Peptidase_M4_C; 1.
Pfam graphical view of domain structure.

PRINTS

PR00730; THERMOLYSIN.

PROSITE

PS00142; ZINC_PROTEASE; 1.

Other

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

Keywords

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

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 24`	`24`	`Potential.`
`PROPEP`	`25 286`	`262`	`Activation peptide.`	`PRO_0000028602`
`CHAIN`	`287 590`	`304`	`Bacillolysin.`	`PRO_0000028603`
`ACT_SITE`	`424 424`		`By similarity.`
`ACT_SITE`	`507 507`		`Proton donor (By similarity).`
`METAL`	`339 339`		`Calcium 1 (Potential).`
`METAL`	`341 341`		`Calcium 1 (Potential).`
`METAL`	`419 419`		`Calcium 2 (Potential).`
`METAL`	`423 423`		`Zinc; catalytic (By similarity).`
`METAL`	`427 427`		`Zinc; catalytic (By similarity).`
`METAL`	`447 447`		`Zinc; catalytic (By similarity).`
`METAL`	`466 466`		`Calcium 2 (Potential).`
`METAL`	`466 466`		`Calcium 3 (Potential).`
`METAL`	`469 469`		`Calcium 4; via carbonyl oxygen (Potential).`
`METAL`	`470 470`		`Calcium 4 (Potential).`
`METAL`	`473 473`		`Calcium 4; via carbonyl oxygen (Potential).`
`METAL`	`476 476`		`Calcium 4 (Potential).`
`CONFLICT`	`287 289`		`NEA -> ATG (in Ref. 1; AA sequence).`

Sequence information

Length: 590 AA [This is the length of the unprocessed precursor]

Molecular weight: 63529 Da [This is the MW of the unprocessed precursor]

CRC64: 4ED303761408F6F3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKVWFSLLG GAMLLGSVAS GASAESSVSG PAQLTPTFHT EQWKAPSSVS GDDIVWSYLN 

        70         80         90        100        110        120 
RQKKSLLGVD SSSVREQFRI VDRTSDKSGV SHYRLKQYVN GIPVYGAEQT IHVGKSGEVT 

       130        140        150        160        170        180 
SYLGAVINED QQEEATQGTT PKISASEAVY TAYKEAAARI EALPTSDDTI SKDAEEPSSV 

       190        200        210        220        230        240 
SKDTYAEAAN NDKTLSVDKD ELSLDKASVL KDSKIEAVEA EKSSIAKIAN LQPEVDPKAE 

       250        260        270        280        290        300 
LYYYPKGDDL LLVYVTEVNV LEPAPLRTRY IIDANDGSIV FQYDIINEAT GKGVLGDSKS 

       310        320        330        340        350        360 
FTTTASGSSY QLKDTTRGNG IVTYTASNRQ SIPGTLLTDA DNVWNDPAGV DAHAYAAKTY 

       370        380        390        400        410        420 
DYYKSKFGRN SIDGRGLQLR STVHYGSRYN NAFWNGSQMT YGDGDGDGST FIAFSGDPDV 

       430        440        450        460        470        480 
VGHELTHGVT EYTSNLEYYG ESGALNEAFS DVIGNDIQRK NWLVGDDIYT PNICGDALRS 

       490        500        510        520        530        540 
MSNPTLYDQP HHYSNLYKGS SDNGGVHTNS GIINKAYYLL AQGGTFHGVT VNGIGRDAAV 

       550        560        570        580        590 
QIYYSAFTNY LTSSSDFSNA RAAVIQAAKD LYGANSAEAT AAAKSFDAVG

P29148 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