ID   NPRV_VIBPR              Reviewed;         609 AA.
AC   Q00971;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Neutral protease;
DE            EC=3.4.24.25;
DE   AltName: Full=Aeromonolysin;
DE   AltName: Full=Vibriolysin;
DE   Flags: Precursor;
GN   Name=nprV;
OS   Vibrio proteolyticus (Aeromonas proteolytica).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=671;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 197-215.
RX   PubMed=1551587; DOI=10.1016/0378-1119(92)90310-l;
RA   David V.A., Deutch A.H., Sloma A., Pawlyk D., Ally A., Durham D.R.;
RT   "Cloning, sequencing and expression of the gene encoding the extracellular
RT   neutral protease, vibriolysin, of Vibrio proteolyticus.";
RL   Gene 112:107-112(1992).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Preferential cleavage of bonds with bulky hydrophobic groups
CC         in P2 and P1'. Phe at P1' is the most favored residue, which
CC         distinguished this enzyme from thermolysin.; EC=3.4.24.25;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; M64809; AAA27548.1; -; Genomic_DNA.
DR   PIR; JT0903; JT0903.
DR   AlphaFoldDB; Q00971; -.
DR   SMR; Q00971; -.
DR   MEROPS; M04.003; -.
DR   KEGG; ag:AAA27548; -.
DR   BRENDA; 3.4.24.25; 167.
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; 1.10.390.10; -; 1.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR025711; PepSY.
DR   InterPro; IPR007280; Peptidase_C_arc/bac.
DR   InterPro; IPR023612; Peptidase_M4.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   InterPro; IPR001570; Peptidase_M4_C_domain.
DR   InterPro; IPR013856; Peptidase_M4_domain.
DR   Pfam; PF07504; FTP; 1.
DR   Pfam; PF03413; PepSY; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   Pfam; PF04151; PPC; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   PROSITE; PS00142; ZINC_PROTEASE; 1.
PE   1: Evidence at protein level;
KW   Calcium; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease; Secreted; Signal; Zinc; Zymogen.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   PROPEP          25..196
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000028630"
FT   CHAIN           197..609
FT                   /note="Neutral protease"
FT                   /id="PRO_0000028631"
FT   ACT_SITE        344
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        426
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         343
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         347
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         367
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   609 AA;  66363 MW;  8FAB1798D737FC42 CRC64;
     MNKTQRHINW LLAVSAATAL PVTAAEMINV NDGSLLNQAL KAQSQSVAPV ETGFKQMKRV
     VLPNGKVKVR YQQTHHGLPV FNTSVVATES KSGSSEVFGV MAQGIADDVS TLTPSVEMKQ
     AISIAKSRFQ QQEKMVAEPA TENEKAELMV RLDDNNQAQL VYLVDFFVAE DHPARPFFFI
     DAQTGEVLQT WDGLNHAQAD GTGPGGNTKT GRYEYGSDFP PFVIDKVGTK CSMNNSAVRT
     VDLNGSTSGN TTYSYTCNDS TNYNDYKAIN GAYSPLNDAH YFGKVVFDMY KDWMNTTPLT
     FQLTMRVHYG NNYENAFWNG SSMTFGDGYS TFYPLVDINV SAHEVSHGFT EQNSGLVYEN
     MSGGMNEAFS DIAGEAAEFY MKGSVDWVVG ADIFKSSGGL RYFDQPSRDG RSIDHASDYY
     NGLNVHYSSG VFNRAFYLLA NKAGWDVRKG FEVFTLANQL YWTANSTFDE GGCGVVKAAS
     DMGYSVADVE DAFNTVGVNA SCGATPPPSG DVLEIGKPLA NLSGNRNDMT YYTFTPSSSS
     SVVIKITGGT GDADLYVKAG SKPTTTSYDC RPYKYGNEEQ CSISAQAGTT YHVMLRGYSN
     YAGVTLRAD