ID   EPRA1_AERHY             Reviewed;         346 AA.
AC   O05485;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Extracellular protease {ECO:0000303|PubMed:9358060};
DE            EC=3.4.24.- {ECO:0000305};
DE   Flags: Precursor;
GN   Name=eprA1 {ECO:0000303|PubMed:9358060};
OS   Aeromonas hydrophila.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=644;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=Ah1;
RX   PubMed=9358060; DOI=10.1016/s0378-1119(97)00371-5;
RA   Chang T.M., Liu C.C., Chang M.C.;
RT   "Cloning and sequence analysis of the gene (eprA1) encoding an
RT   extracellular protease from Aeromonas hydrophila.";
RL   Gene 199:225-229(1997).
CC   -!- FUNCTION: Heat-labile protease. {ECO:0000269|PubMed:9358060}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P81054};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P81054};
CC   -!- SIMILARITY: Belongs to the peptidase M35 family. {ECO:0000305}.
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DR   EMBL; U93600; AAB88221.1; -; Genomic_DNA.
DR   RefSeq; WP_029314738.1; NZ_UETG01000009.1.
DR   AlphaFoldDB; O05485; -.
DR   SMR; O05485; -.
DR   STRING; 1448139.AI20_05875; -.
DR   MEROPS; M35.003; -.
DR   eggNOG; COG4104; Bacteria.
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   CDD; cd11306; M35_peptidyl-Lys; 1.
DR   Gene3D; 3.40.390.10; -; 1.
DR   InterPro; IPR029463; Lys_MEP.
DR   InterPro; IPR034115; M35_peptidyl-Lys.
DR   InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR   Pfam; PF14521; Aspzincin_M35; 1.
DR   SMART; SM01351; Aspzincin_M35; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Protease; Signal; Zinc.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..346
FT                   /note="Extracellular protease"
FT                   /id="PRO_0000029240"
FT   ACT_SITE        297
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         296
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         300
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
FT   BINDING         309
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P81054"
SQ   SEQUENCE   346 AA;  37298 MW;  276E20F51F88B8B4 CRC64;
     MMKATPIALL LAGVLASPLC AAGLDARLTL VEGSTDDVRV NLTLTNTGEK PVRLLKWQLP
     GSEDAPLFQV ERDGQPVDYE GALIKRAAPS DKDYQLLKAG QSLTVQAEVS GLYDMSAQGQ
     YSIRYLLPTV AQEGKAAKAK QAQASESNAV TLWVDGVSDD RVLAKAAVAE PQAVSASVSF
     SGRCTNTQKS DILAALDAAS GIANNSSSYL AVDKPNGQRY RSWFGAYDAT RWNQAETNFS
     KIKDAIDNKP LTFDCGCKQS YFAYVYPDQP YKVYLCKSFW TAPVTGTDSR AGTIVHELSH
     FNVVAGTDDL GYGQANARNL ASTDPQKALN NADNHEYFAE NTPSEN