ID   E8LUQ3_9VIBR            Unreviewed;       924 AA.
AC   E8LUQ3;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
DE   RecName: Full=Protease 3 {ECO:0000256|ARBA:ARBA00017565};
DE            EC=3.4.24.55 {ECO:0000256|ARBA:ARBA00012449};
DE   AltName: Full=Pitrilysin {ECO:0000256|ARBA:ARBA00033450};
DE   AltName: Full=Protease III {ECO:0000256|ARBA:ARBA00031184};
DE   AltName: Full=Protease pi {ECO:0000256|ARBA:ARBA00029597};
GN   ORFNames=VIBR0546_07512 {ECO:0000313|EMBL:EGA65549.1};
OS   Vibrio brasiliensis LMG 20546.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio; Vibrio oreintalis group.
OX   NCBI_TaxID=945543 {ECO:0000313|EMBL:EGA65549.1, ECO:0000313|Proteomes:UP000004371};
RN   [1] {ECO:0000313|EMBL:EGA65549.1, ECO:0000313|Proteomes:UP000004371}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 20546 {ECO:0000313|EMBL:EGA65549.1,
RC   ECO:0000313|Proteomes:UP000004371};
RX   PubMed=21930677; DOI=10.1099/ijs.0.032375-0;
RA   Hoffmann M., Monday S.R., Allard M.W., Strain E.A., Whittaker P., Naum M.,
RA   McCarthy P.J., Lopez J.V., Fischer M., Brown E.W.;
RT   "Vibrio caribbeanicus sp. nov., isolated from the marine sponge
RT   Scleritoderma cyanea.";
RL   Int. J. Syst. Evol. Microbiol. 62:1736-1743(2012).
CC   -!- FUNCTION: Endopeptidase that degrades small peptides of less than 7
CC       kDa, such as glucagon and insulin. {ECO:0000256|ARBA:ARBA00002184}.
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGA65549.1}.
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; AEVS01000070; EGA65549.1; -; Genomic_DNA.
DR   RefSeq; WP_006879565.1; NZ_AEVS01000070.1.
DR   AlphaFoldDB; E8LUQ3; -.
DR   STRING; 945543.VIBR0546_07512; -.
DR   MEROPS; M16.008; -.
DR   eggNOG; COG1025; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000004371; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 4.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   InterPro; IPR032632; Peptidase_M16_M.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   Pfam; PF16187; Peptidase_M16_M; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          182..358
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          366..642
FT                   /note="Peptidase M16 middle/third"
FT                   /evidence="ECO:0000259|Pfam:PF16187"
FT   DOMAIN          647..817
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   924 AA;  105645 MW;  C68FDC09AC711ACF CRC64;
     MHISPNDTNK YRYLTLANGI RVLLIHDSSA QKSAAALAVN VGHFDDPQDR EGLAHYLEHM
     LFLGTEKYPK VGEFQSYINQ HGGSNNAWTG TEHTCFFFDV THNAFESGLD RFSQFFTAPL
     FNSEALDKER QAVESEYKLK LKDDSRRLYQ VHKELVNPEH PFSKFSVGNL ETLGDRDGQS
     IRDEIVAFHF EQYSADLMTL AITGPQQLDQ LESWCIEKFT AIPNHHLIDK QIEVPYCDEH
     STGIMVNVEP VKEIRKLIMT FPMPSMDQHY QSKPLSYFAH LLGYEGSGSL MLALKGQGWI
     TSLSAGGGTS GSNYREFTVS CALTPKGLEH TDEIIQAVFS YLNLIKKDGM AEWRYLEKQA
     VLESAFRFQE PTRPLDLVSH LVINMQHYGE KDVIYGDFMM NHYDEPLLNT LFEFFAPENL
     RTTLVAKGYD YPNRAKWYFT PYGITEFSDR QKEFFLQTSQ LNFSLPEKNP FICFDLDPKE
     IETPHETPQV LEELPGFKLW HLQDVEFRVP KGVIYIAIDS PHAVANPRNI VKTRLCVEMF
     LDSLATDTYQ AEIAGMGYNM YAHQGGVTLT ISGFSQKQPE LMQLILSRFA ERDFSATRFD
     NIKQQLLRNW QNSAQDRPIS QLFNALTGIL QPNNPPYSAL VEALETIEVD ELASFVDAIL
     AELHVEMFVY GDWTKADALS LGSTLKDALR VHNQQYEEAL RPLVMLGKNG SFQREVFCDQ
     EDSATVLYYQ CDDTSPRSIA LYSLANHLMS ATFFHEIRTK QQLGYMVGTG NLPLNRHPGI
     ALYVQSPNAA PIELIRSIDE FLNAFYMVLL ELNEYQWHSS KRGLWNQIAT PDTTLRGRAQ
     RLWVAIGNKD TEFNQREVVL EELKTLTRTD MIRFVVNELK PRTANRLIMH TQGNAHHESE
     RLDLGLEIGS VEEFQLRPKD VELG
//