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Database: UniProt
Entry: A0A0M0HUH8_VIBNE
LinkDB: A0A0M0HUH8_VIBNE
Original site: A0A0M0HUH8_VIBNE 
ID   A0A0M0HUH8_VIBNE        Unreviewed;       596 AA.
AC   A0A0M0HUH8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:KOO05512.1};
GN   ORFNames=AKJ17_01600 {ECO:0000313|EMBL:KOO05512.1};
OS   Vibrio nereis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=693 {ECO:0000313|EMBL:KOO05512.1, ECO:0000313|Proteomes:UP000037515};
RN   [1] {ECO:0000313|Proteomes:UP000037515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19584 {ECO:0000313|Proteomes:UP000037515};
RA   Giubergia S., Machado H., Mateiu R.V., Gram L.;
RT   "Vibrio galatheae sp. nov., a novel member of the Vibrionaceae family
RT   isolated from the Solomon Islands.";
RL   Submitted (AUG-2015) 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:KOO05512.1}.
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DR   EMBL; LHPJ01000001; KOO05512.1; -; Genomic_DNA.
DR   RefSeq; WP_053394026.1; NZ_LHPJ01000001.1.
DR   AlphaFoldDB; A0A0M0HUH8; -.
DR   STRING; 693.AKJ17_01600; -.
DR   PATRIC; fig|693.5.peg.322; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000037515; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09607; M3B_PepF; 1.
DR   Gene3D; 1.10.1370.20; Oligoendopeptidase f, C-terminal domain; 1.
DR   Gene3D; 1.20.140.70; Oligopeptidase f, N-terminal domain; 1.
DR   InterPro; IPR034006; M3B_PepF_2.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR011977; Pept_M3B_clade3.
DR   InterPro; IPR001333; Peptidase_M32_Taq.
DR   NCBIfam; TIGR02290; M3_fam_3; 1.
DR   PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR   PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR   Pfam; PF01432; Peptidase_M3; 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:UP000037515};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          203..578
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  67332 MW;  EC5C15DF086C1E2A CRC64;
     MTTPKWDLSI AYQGLSDSKI SQDIELIQQC IETLTLHTDS RTSVSVMQNA IQTREAAGKL
     LATINTFAQC HASVDASNGD AKSLVGRLAK LNSQLSQAFT PYQDALVTQP ESFIQEVLAH
     ESEDVSGQGF QIFTERKLAD TKLGIAEEQL MSALEVDGKD AWGRLYDNIT GSLQVTLENE
     EKAKVGLSKA ASTLYGTDFE AQKPAWLGIQ NAMRQHQESF AAILNALAGW RLTEYQKRSK
     VRDVHFLEAS LHGSRIEQTT LDAMISTAKA NRHVGQKAGK LMARVHGLEQ MAPWNHLAGM
     PSLTDAEPKV YEFDEAIDII RSAFSTVDPE MAEFVTLMVK NGWIDAAPTE NRRLGAYCTK
     FAATRTPLVF MTWGGSRSHL LTLAHEIGHA FHNWVMRDMP LCQTRYPMTL AETASIFAEN
     TVRDYLLGQA ETREEKLEML WEELSSCYAL MVNIPVRYEF EKSFYEKRAE GELEAGQLCD
     LMSETWKEWY GDSMSEPDPY FWASKLHFSI SQVSFYNYPY LFGYLFSIGV YAQRESKGEQ
     FYQDYVNLLR DTGSMMAEDV VQKHLGMDLS SQEFWQQSID RVASKIDEFE SLLDQL
//
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