Reviewed, UniProtKB/Swiss-Prot P27458 (PRLB_ACHLY)

Names and origin

Protein names	Recommended name:     Beta-lytic metalloendopeptidase     EC=3.4.24.32 Alternative name(s):     Beta-lytic protease
Organism	Achromobacter lyticus
Taxonomic identifier	224 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Achromobacter

Protein attributes

Sequence length	374 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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.
Sequence similarities	Belongs to the peptidase M23A family.

Ontologies

Keywords
Cellular component	Secreted
Domain	Signal
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Disulfide bond Zymogen
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	proteolysis Inferred from electronic annotation. Source: InterPro
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	metalloendopeptidase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 24	24
	Propeptide	25 – 195	171	Ref.1		PRO_0000026810
	Chain	196 – 374	179	Beta-lytic metalloendopeptidase		PRO_0000026811
Sites
	Metal binding	316	1	Zinc Potential
	Metal binding	318	1	Zinc Potential
Amino acid modifications
	Disulfide bond	261 ↔ 307		By similarity
	Disulfide bond	351 ↔ 364		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P27458-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 431E51B84575DE14	FASTA	374	40,085
	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

References

[1]	"Molecular cloning and nucleotide sequence of the beta-lytic protease gene from Achromobacter lyticus." Li S.L., Norioka S., Sakiyama F. J. Bacteriol. 172:6506-6511(1990) [PubMed: 2228973] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 196-220. Strain: M497-1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60896 Genomic DNA. Translation: AAA21906.1.
PIR	LYYXLY. A37151.
3D structure databases
ModBase	Search...
Protein family/group databases
MEROPS	M23.001.
Enzyme and pathway databases
BRENDA	3.4.24.32. 19051.
Family and domain databases
InterPro	IPR000841. Pept_M23A_Blytic. [Graphical view]
PRINTS	PR00933. BLYTICPTASE.
ProtoNet	Search...

Entry information

Entry name

PRLB_ACHLY

Accession

Primary (citable) accession number: P27458

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 46 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)