ID   A0A090TWD3_9VIBR        Unreviewed;       481 AA.
AC   A0A090TWD3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:GAL35232.1};
GN   ORFNames=JCM19240_3602 {ECO:0000313|EMBL:GAL35232.1};
OS   Vibrio maritimus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=990268 {ECO:0000313|EMBL:GAL35232.1, ECO:0000313|Proteomes:UP000029224};
RN   [1] {ECO:0000313|EMBL:GAL35232.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL35232.1,
RC   ECO:0000313|Proteomes:UP000029224};
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RT   "Vibrio maritimus JCM 19240. (C210) whole genome shotgun sequence.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:GAL35232.1, ECO:0000313|Proteomes:UP000029224}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 19240 {ECO:0000313|EMBL:GAL35232.1,
RC   ECO:0000313|Proteomes:UP000029224};
RG   NBRP consortium;
RA   Sawabe T., Meirelles P., Nakanishi M., Sayaka M., Hattori M., Ohkuma M.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:GAL35232.1}.
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DR   EMBL; BBMT01000006; GAL35232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A090TWD3; -.
DR   Proteomes; UP000029224; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.30; -; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029224};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          115..173
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..447
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   481 AA;  53483 MW;  212A13726AC72F52 CRC64;
     MKNAVWDLSI AYQGLNDPKV EQDIELIQRS ISLLTHHQEE RQHVVAMQNA IQTMEAASTL
     LNTVSTLANC HASTNAQNTQ AKQLIGRLSQ LSSELEQAFS PYENVLAFAD VAFIQQVLDH
     DNPSVAGQGF QIELLQRKAQ TQLSIAEEQL LSAMQVDGRD AWGRLYDNIT GSLSITIDTE
     QGTETLGFSA AASLLYGGEF AKQEAAWKGI QSAMKANDTS FAAIVNALAG WRHNEGKKRS
     HNSEEHFLDP SLRANRIQRE TLEAMMSVAK KHRAIGQKAG KLMAKVHGLP SMTPWNHLAA
     MPPLGNGEAK VYEFAEGIEV IKCAFEQVNP EMAEFVQTMV DNGWIDAAPS ENRRLGAYCT
     QLAATRTPLV FMTWGGSRSD LLTLAHELGH AFHNWVMRDL PLCRTSYPMT LAETASIFAE
     NIVRDYLLEQ AKTSEEKLEM LWEELSSAYA SPSIFRFVLS LKKRSIKHAK RVNLMQTSYV
     S
//