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 27-MAR-2024, entry version 118.
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; Pseudomonadota; 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.AA407_15075; -.
DR MEROPS; M04.003; -.
DR OMA; RHKRTTL; -.
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 CDD; cd09597; M4_TLP; 1.
DR Gene3D; 2.60.120.380; -; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 3.10.450.40; -; 1.
DR Gene3D; 3.10.450.490; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
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 PANTHER; PTHR33794; BACILLOLYSIN; 1.
DR PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR Pfam; PF04151; PPC; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF89260; Collagen-binding domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
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
//
