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Database: UniProt
Entry: A0A0R2DDR8_9LACO
LinkDB: A0A0R2DDR8_9LACO
Original site: A0A0R2DDR8_9LACO 
ID   A0A0R2DDR8_9LACO        Unreviewed;       601 AA.
AC   A0A0R2DDR8;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, 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   ORFNames=FD13_GL000236 {ECO:0000313|EMBL:KRN02097.1};
OS   Levilactobacillus senmaizukei DSM 21775 = NBRC 103853.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Levilactobacillus.
OX   NCBI_TaxID=1423803 {ECO:0000313|EMBL:KRN02097.1, ECO:0000313|Proteomes:UP000051589};
RN   [1] {ECO:0000313|EMBL:KRN02097.1, ECO:0000313|Proteomes:UP000051589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21775 {ECO:0000313|EMBL:KRN02097.1,
RC   ECO:0000313|Proteomes:UP000051589};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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   -!- 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:KRN02097.1}.
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DR   EMBL; AYZH01000010; KRN02097.1; -; Genomic_DNA.
DR   RefSeq; WP_061776491.1; NZ_BCWD01000009.1.
DR   AlphaFoldDB; A0A0R2DDR8; -.
DR   STRING; 1423803.FD13_GL000236; -.
DR   PATRIC; fig|1423803.3.peg.230; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000051589; 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   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          114..183
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          204..584
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   601 AA;  67565 MW;  F6759BD1CA7991CE CRC64;
     MKQLPQRSAV PENLTWDLTS IYPDDANFRT AVQQVKAAAD QINSLSGQLS KSGADLYRVT
     MAILDLNRQL ERLYVYASLK NDQDTSNAVY QDLADQAESL VATVASATAW YEPEVLALSA
     TDLQNLIDSE PKLADFQHFF DVLAEQREHT LSTSEEKLLA GAQDIFGASA KTYSVLSDAD
     LKFPVVQDAE GKDVRLSEGL YGVLLQSTTP RVREQAFKGL YSVYQQFRHT FAATLSSEVK
     THNFMAKTRH YTSAREAAMA DNQIPAKVYD NLVTTVNNHL DSLHDYVRLR RGILGLPELH
     MYDLYTPITG EPSLTYTYEE AQQEALKALS VLGPDYIDQV QAMFTGRAID VVENQGKRTG
     AYSGGAYDTK PYILLNWQDS LESLFTLVHE MGHSMHSHYT RSNQPFQYGD YSIFVAEIAS
     TTNENLLTDY LLKTQTDPKV RAYVLNHYLD GFKGTVYRQT QFAEFEDFIH QQAAAGQSLT
     ADFMSDFYGK LNQRYYGDAV VSDPEIADEW TRIPHFYYNY YVYQYATGFA AATTLAQRIL
     SGDPTKREAY LGYLKAGNSA APLDVMRSAG VDMTKPDYLE TAFATFDKRL AEFKGLAKQL
     K
//
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