ID   EMPA_VIBAN              Reviewed;         611 AA.
AC   P43147;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Virulence metalloprotease;
DE            EC=3.4.24.-;
DE   AltName: Full=Vibriolysin;
DE   Flags: Precursor;
GN   Name=empA;
OS   Vibrio anguillarum (Listonella anguillarum).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=55601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=NB10 / Serotype O1;
RX   PubMed=1429449; DOI=10.1128/jb.174.22.7235-7244.1992;
RA   Milton D.L., Norqvist A., Wolf-Watz H.;
RT   "Cloning of a metalloprotease gene involved in the virulence mechanism of
RT   Vibrio anguillarum.";
RL   J. Bacteriol. 174:7235-7244(1992).
RN   [2]
RP   PROTEIN SEQUENCE OF 200-219.
RX   PubMed=2228244; DOI=10.1128/iai.58.11.3731-3736.1990;
RA   Norqvist A., Norrman B., Wolf-Watz H.;
RT   "Identification and characterization of a zinc metalloprotease associated
RT   with invasion by the fish pathogen Vibrio anguillarum.";
RL   Infect. Immun. 58:3731-3736(1990).
CC   -!- FUNCTION: Extracellular zinc metalloprotease involved in the virulence
CC       mechanism of V.anguillarum.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Seems to be more extensively processed.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family. {ECO:0000305}.
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DR   EMBL; L02528; AAA27517.1; -; Genomic_DNA.
DR   PIR; A47015; A47015.
DR   RefSeq; WP_013868121.1; NZ_VSLF01000016.1.
DR   AlphaFoldDB; P43147; -.
DR   SMR; P43147; -.
DR   STRING; 55601.VANGNB10_cII0919c; -.
DR   MEROPS; M04.003; -.
DR   OMA; QLYWTAN; -.
DR   OrthoDB; 1465483at2; -.
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; Virulence; Zinc; Zymogen.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000255"
FT   PROPEP          26..199
FT                   /evidence="ECO:0000269|PubMed:2228244"
FT                   /id="PRO_0000028626"
FT   CHAIN           200..611
FT                   /note="Virulence metalloprotease"
FT                   /id="PRO_0000028627"
FT   ACT_SITE        347
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   ACT_SITE        429
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         346
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         350
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT   BINDING         370
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ   SEQUENCE   611 AA;  66726 MW;  93A9212B798B8A8B CRC64;
     MKKVQRQMKW LFLAASISAA LPVSAAKMVQ VDDPSLLEQA LSMQARSIVP TQNGFQVVKS
     VTLPNGKVKV RYQQMYHGLP VFNTSVVATQ TEKGIGQVYG MLAQQIDSDV VSTSPQVEQK
     QAVSIALTHY QQQNPSLTSA DLVTENERAQ LMVRLDENQM AQMVYLVDFF VATNEPARPF
     FFIDANSGDV LQTWEGLNHA EATGTGPGGN QKTGFYQYGT DFPGLVINKV GNTCSMMNSA
     VKTVDMKHAT SGGSTFSYSC TDASNYNDYK AINGAYSPLN DAHYFGKVVF DMYKDWMNTT
     PLTFQLTMRV HYDSNYENAF WNGSSMTFGD GQNTFYPLVD INVSAHEVSH GFTEQNSGLV
     YQNMSGGINE AFSDIAGEAA EFYMKGSVDW VVGSDIFKSS GGLRYFDQPS KDGRSIDHAS
     QYYNGLNVHY SSGVFNRAYY LLANKANWSV RKGFEVFTVA NQLYWTANST FDQGGCGVAK
     AAQDLGYNKA DVVDAFNQVG VNASCGVVPP TENVLEKGKP VIGLQGTRSS EAFYTFTVAS
     STSAKVSISL GSGDADLYVK AGSKPTTSSW DCRPYKSGNN EQCTISATPG TTYHVMLKGY
     SNYSGVTLRL D