NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 196-220.
STRAIN=M497-1;
PubMed=2228973 [NCBI, ExPASy, EBI, Israel, Japan]
Li S.L., Norioka S., Sakiyama F.;
"Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus.";
J. Bacteriol. 172:6506-6511(1990).

Comments

CATALYTIC ACTIVITY: Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO₃H).
COFACTOR: Binds 1 zinc ion per subunit.
SUBCELLULAR LOCATION: Secreted.
SIMILARITY: Belongs to the peptidase M23A 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

M60896; AAA21906.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A37151; LYYXLY.

3D structure databases

ModBase

P27458.

Protein family/group databases

MEROPS

M23.001; -.

Ontologies

GO:0005576;	Cellular component: extracellular region (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 UniProtKB-KW).
GO:0006508;	Biological process: proteolysis (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

InterPro

IPR000841; Pept_M23A_Blytic.
Graphical view of domain structure.

PRINTS

PR00933; BLYTICPTASE.

Other

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

Keywords

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`
`PROPEP`	`25 195`	`171`		`PRO_0000026810`
`CHAIN`	`196 374`	`179`	`Beta-lytic metalloendopeptidase.`	`PRO_0000026811`
`METAL`	`316 316`		`Zinc (Potential).`
`METAL`	`318 318`		`Zinc (Potential).`
`DISULFID`	`261 307`		`By similarity.`
`DISULFID`	`351 364`		`By similarity.`

Sequence information

Length: 374 AA [This is the length of the unprocessed precursor]

Molecular weight: 40085 Da [This is the MW of the unprocessed precursor]

CRC64: 431E51B84575DE14 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKISKAGLG LALVCALATI GGNAARRATA QRRGSGVFYD EMFDFDIDAH LAKHAPHLHK 

        70         80         90        100        110        120 
HSEEISHWAG YSGISRSVDR ADGAAERAVT PSARRIVRSA SWRAPTASAR RPARSRWRCA 

       130        140        150        160        170        180 
SRCTSAIPTR QGAGDAGPRQ SAAGAVRAFR RQRAGGRAAR RRRVPAGLRP PVQRTAPGQG 

       190        200        210        220        230        240 
GFGPLRQGRP GRAAVSPNGL LQFPFPRGAS WHVGGAHTNT GSGNYPMSSL DMSRGGGWGS 

       250        260        270        280        290        300 
NQNGNWVSAS AAGSFKRHSS CFAEIVHTGG WSTTYYHLMN IQYNTGANVS MNTAIANPAN 

       310        320        330        340        350        360 
TQAQALCNGG QSTGPHEHWS LKQNGSFYHL NGTYLSGYRI TATGSSYDTN CSRFYLTKNG 

       370 
QNYCYGYYVN PGPN

P27458 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