ID   A0A069CSP0_WEIOS        Unreviewed;       607 AA.
AC   A0A069CSP0;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF {ECO:0000313|EMBL:GAK30248.1};
GN   ORFNames=WOSG25_020430 {ECO:0000313|EMBL:GAK30248.1};
OS   Weissella oryzae (strain DSM 25784 / JCM 18191 / LMG 30913 / SG25).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae; Weissella.
OX   NCBI_TaxID=1329250 {ECO:0000313|EMBL:GAK30248.1, ECO:0000313|Proteomes:UP000030643};
RN   [1] {ECO:0000313|Proteomes:UP000030643}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25784 / JCM 18191 / LMG 30913 / SG25
RC   {ECO:0000313|Proteomes:UP000030643};
RX   PubMed=25013139; DOI=10.1128/genomea.00667-14;
RA   Tanizawa Y., Fujisawa T., Mochizuki T., Kaminuma E., Suzuki Y.,
RA   Nakamura Y., Tohno M.;
RT   "Draft genome sequence of Weissella oryzae SG25T, isolated from fermented
RT   rice grains.";
RL   Genome Announc. 2:0-0(2014).
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}.
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DR   EMBL; DF820485; GAK30248.1; -; Genomic_DNA.
DR   RefSeq; WP_027698370.1; NZ_DF820485.1.
DR   AlphaFoldDB; A0A069CSP0; -.
DR   STRING; 1329250.WOSG25_020430; -.
DR   MEROPS; M03.007; -.
DR   eggNOG; COG1164; Bacteria.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000030643; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000030643};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          117..184
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          205..585
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   607 AA;  68351 MW;  C206C77DD0E55801 CRC64;
     MAKKLPIRTE VPLAMTWDLT TIFKDDDAWQ AAYDDLEDRL AGANVLAENA DASAANLLVA
     LKYGLGLMRD LERIYVYASM KSDQDTNNNF YQGLAAKAGA LAAKVSAAIA FFDPLVLSLP
     AEKLTAYFAE EPELQSYQHY FDSILTQRGH LLSSDEERLL AAASDVFGAS ERTFGILDNA
     DLKFGTVIDD AGDEVQLSNG VYSQLLESPI RKVREETFKT FYQSYIDLEN TFASLLAGNV
     KSQNFNAQVH NYGSAREAAL ARNHVPEQVY DNLVTEVNKA LPLLHRYVAL RKKLLNLKEL
     HSYDLYTPIL GTPDYEIDFE GAKAEALQAL APLGDDYLAV VNTAFDNRWI DVVENQGKRS
     GAYSGGSYDT NPFILLNWQD NLNNLDTLVH EMGHSVHSYF TRQNQPYHYG DYPIFLAEIA
     STTNENLLTD YLLNSLDDKK LKAYILNQFL DGVKGTVFRQ TQFAEFEQWM HVQDAAGVPL
     TAEVLDDAYA ELNQRYYGPE LMIDEEIAHE WERIPHFYYN FYVYQYSTGF AAAVAMSDKI
     LHGGEKAVIE YKNYLKAGSS ADPIDVMKAA GLDMTKPDYL QDTFRLFEER LTEFESVVAE
     LEATDQL
//