ID   E3BGU2_9VIBR            Unreviewed;       924 AA.
AC   E3BGU2;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 41.
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=VIBC2010_13924 {ECO:0000313|EMBL:EFP97749.1};
OS   Vibrio caribbeanicus ATCC BAA-2122.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=796620 {ECO:0000313|EMBL:EFP97749.1, ECO:0000313|Proteomes:UP000002943};
RN   [1] {ECO:0000313|EMBL:EFP97749.1, ECO:0000313|Proteomes:UP000002943}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2122 {ECO:0000313|EMBL:EFP97749.1,
RC   ECO:0000313|Proteomes:UP000002943};
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:EFP97749.1}.
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DR   EMBL; AEIU01000050; EFP97749.1; -; Genomic_DNA.
DR   RefSeq; WP_009600186.1; NZ_AEIU01000050.1.
DR   AlphaFoldDB; E3BGU2; -.
DR   STRING; 796620.VIBC2010_13924; -.
DR   eggNOG; COG1025; Bacteria.
DR   OrthoDB; 9811314at2; -.
DR   Proteomes; UP000002943; 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   Reference proteome {ECO:0000313|Proteomes:UP000002943};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          21..158
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          183..361
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          648..822
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   924 AA;  105410 MW;  96C2255F1341F0F5 CRC64;
     MHISPNDTNQ YRHITLSNGL RVLLVHDHTA KKSAAAVAVN VGHFDDPTDR QGLSHFLEHM
     LFLGTEKYPE VGDFQNYVSQ HGGQNNAWTG TEHTCYFFDI LPNAFYRGLD RFSQFFISPL
     FNPEALDKER QAVESEYRLK YKEDSRRLYQ VHKEVINPAH PFSKFSVGNM ETLGDRSGES
     IRPEIVEFYS SQYSSDIMTL VLLGPQTLNE LEKWADELFS AISNKSAAGK VIKVPYKDSN
     STPIFVAVEP LKEIRKLIVT FPLPSIDKYY RSKPLSYIAH LLGYEGKGSL MLALKEKGWI
     TSLSAGGGTS GSNYREFTIN CTLTLDGLAF VDSIVQAIFN FISLIKTSGV EEWRYQEKKS
     VLEAAFQFRE PANALDLVSH LVVNMQHYSS EDIIYGDYMM MEFDEEQIRS LLDFFNPSNM
     RLTLLSKGQH YSNQAKWYDT PYSVSKITAS QIKNYTHSSD LELQLPEANP FICNVLKAKP
     LETLNPTPTV IDELPGFKLW HMQDNEFRVP KGVVYIAIDS PYAVSNPSNI VKTRLCVEMF
     LDSLSVDTYQ AEIAGMGYTM YTHQGGVTLT VSGFTQKQEK LIKTILDRFN QRDFDPTRFE
     NIKNQLMRNW KNSAQDRPLS QLFSALTGIL QPNNPPYSTL VKELEMIEVD ELASFVSNVL
     ATLHVEMFVF GDWTQSDALS LGTMIKDALR VKNQRYEEAL RPLIMLGKNG TFEHEVRCEQ
     DDSATVVYYQ CDDTSPRSIA LYSLANHLMS ATFFHEIRTK QQLGYMVGTG NLPLNRHPGI
     VLYVQSPKVA PINLMASIDE FLNAFHLVLM ELDEYQWHSS KKGLWNQISV PDKTLRGRAQ
     RLWVAIGNKD HFFDQKEKVL EELKNLSRAD MIRFVIDELK PRTANRLIMH SKGNSHQEEK
     NLDIGIQIGS IDEFQLRPRD IELG
//