ID   U5S7Y6_9LACT            Unreviewed;       605 AA.
AC   U5S7Y6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=Q783_03360 {ECO:0000313|EMBL:AGY81340.1};
OS   Carnobacterium inhibens subsp. gilichinskyi.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY81340.1, ECO:0000313|Proteomes:UP000017469};
RN   [1] {ECO:0000313|EMBL:AGY81340.1, ECO:0000313|Proteomes:UP000017469}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WN1359 {ECO:0000313|EMBL:AGY81340.1,
RC   ECO:0000313|Proteomes:UP000017469};
RX   PubMed=24285647;
RA   Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT   "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT   (DSM 27470T).";
RL   Genome Announc. 1:e00985-13(2013).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides. {ECO:0000256|RuleBase:RU368091}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU368091};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU368091};
CC   -!- SIMILARITY: Belongs to the peptidase M3B family.
CC       {ECO:0000256|RuleBase:RU368091}.
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; CP006812; AGY81340.1; -; Genomic_DNA.
DR   RefSeq; WP_023177325.1; NC_022606.1.
DR   AlphaFoldDB; U5S7Y6; -.
DR   STRING; 1266845.Q783_03360; -.
DR   MEROPS; M03.007; -.
DR   KEGG; caw:Q783_03360; -.
DR   PATRIC; fig|1266845.5.peg.614; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   Proteomes; UP000017469; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd09608; 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   Gene3D; 1.10.287.830; putative peptidase helix hairpin domain like; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   NCBIfam; TIGR00181; pepF; 1.
DR   PANTHER; PTHR11804:SF79; MITOCHONDRIAL INTERMEDIATE PEPTIDASE; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
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|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368091};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368091};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU368091};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU368091};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          117..186
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          207..587
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  69787 MW;  11AF2428D8A1F64E CRC64;
     MSESKKLPKR NEVPSEWTWD LEVVFKSDDD FTLSYKELET KVKTVVSYKG TLNEGSKSFL
     KAIQAILDLS NQLETIYVYA QLKNDQDTTN STYQGMYEQA TKLATQANEA ISWFEPEVLE
     LSEETLARYF NENDDLAIYK HFIDQLTAAR KHVLSANEEA LLAGAGEIFN ASSRTFNILN
     NADITFPTIK DENGNDIQLS HGVYGQLMES TDRSVREAAF KNLYKVYDGL QNTFSSTLSS
     HVKYHNYNAK VHHYDSAREK ALSSNHIPES VYDTLLDVVH EHLPLLHRYV ALRKELLNVE
     ELHMYDMYTP ISGEAGIKYT YEEAEAETMK ALKPLGEEYL SVLKKAFNNR WIDVMENEGK
     RSGAYSSGAY ETNPYILLNW HDSLNHLYTL VHELGHSVHS YYTRTNQPYV YGDYSIFLAE
     IASTTNENIL TDYLLETQKD PKVRAYVLNH YLDGFKGTIF RQTQFAEFEH FIHEEAAKGT
     PLTSEFLNNY YGELNARYYG PDVEKDPEIA LEWTRIPHFY YNYYVYQYST GFSAATALAD
     KIVKDEDRAL DNYLTYLKSG NSDYPIEVMK KAGVDMTEKT YIEDAMKVFE TRLNELEELI
     ETLKD
//