ID   PRLB_ACHLY              Reviewed;         374 AA.
AC   P27458;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Beta-lytic metalloendopeptidase;
DE            EC=3.4.24.32;
DE   AltName: Full=Beta-lytic protease;
DE   Flags: Precursor;
OS   Achromobacter lyticus.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=224;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 196-220.
RC   STRAIN=M497-1;
RX   PubMed=2228973; DOI=10.1128/jb.172.11.6506-6511.1990;
RA   Li S.L., Norioka S., Sakiyama F.;
RT   "Molecular cloning and nucleotide sequence of the beta-lytic protease gene
RT   from Achromobacter lyticus.";
RL   J. Bacteriol. 172:6506-6511(1990).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cleavage of N-acetylmuramoyl-|-Ala, and of the insulin B chain
CC         at 23-Gly-|-Phe-24 > 18-Val-|-Cys(SO3H).; EC=3.4.24.32;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC       Note=Binds 1 zinc ion per subunit.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M23A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; M60896; AAA21906.1; -; Genomic_DNA.
DR   PIR; A37151; LYYXLY.
DR   AlphaFoldDB; P27458; -.
DR   SMR; P27458; -.
DR   MEROPS; M23.001; -.
DR   KEGG; ag:AAA21906; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR000841; Pept_M23A_Blytic.
DR   PRINTS; PR00933; BLYTICPTASE.
DR   SUPFAM; SSF51261; SSF51261; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..24
FT   PROPEP          25..195
FT                   /evidence="ECO:0000269|PubMed:2228973"
FT                   /id="PRO_0000026810"
FT   CHAIN           196..374
FT                   /note="Beta-lytic metalloendopeptidase"
FT                   /id="PRO_0000026811"
FT   REGION          128..187
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         316
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         318
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   DISULFID        261..307
FT                   /evidence="ECO:0000250"
FT   DISULFID        351..364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   374 AA;  40085 MW;  431E51B84575DE14 CRC64;
     MKKISKAGLG LALVCALATI GGNAARRATA QRRGSGVFYD EMFDFDIDAH LAKHAPHLHK
     HSEEISHWAG YSGISRSVDR ADGAAERAVT PSARRIVRSA SWRAPTASAR RPARSRWRCA
     SRCTSAIPTR QGAGDAGPRQ SAAGAVRAFR RQRAGGRAAR RRRVPAGLRP PVQRTAPGQG
     GFGPLRQGRP GRAAVSPNGL LQFPFPRGAS WHVGGAHTNT GSGNYPMSSL DMSRGGGWGS
     NQNGNWVSAS AAGSFKRHSS CFAEIVHTGG WSTTYYHLMN IQYNTGANVS MNTAIANPAN
     TQAQALCNGG QSTGPHEHWS LKQNGSFYHL NGTYLSGYRI TATGSSYDTN CSRFYLTKNG
     QNYCYGYYVN PGPN