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Database: UniProt
Entry: A0A0R2MS08_9LACO
LinkDB: A0A0R2MS08_9LACO
Original site: A0A0R2MS08_9LACO 
ID   A0A0R2MS08_9LACO        Unreviewed;       605 AA.
AC   A0A0R2MS08;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=IV56_GL001139 {ECO:0000313|EMBL:KRO16358.1};
OS   Lacticaseibacillus saniviri JCM 17471 = DSM 24301.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1293598 {ECO:0000313|EMBL:KRO16358.1, ECO:0000313|Proteomes:UP000050969};
RN   [1] {ECO:0000313|EMBL:KRO16358.1, ECO:0000313|Proteomes:UP000050969}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24301 {ECO:0000313|EMBL:KRO16358.1,
RC   ECO:0000313|Proteomes:UP000050969};
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:KRO16358.1}.
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DR   EMBL; JQCE01000038; KRO16358.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R2MS08; -.
DR   STRING; 1293598.IV56_GL001139; -.
DR   PATRIC; fig|1293598.4.peg.1202; -.
DR   Proteomes; UP000050969; 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:UP000050969};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          117..185
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          206..586
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  68193 MW;  999FA1358ED4C5A4 CRC64;
     MYAMQQLPLR NEVPEPLTWD LTTIFASDQD WEQALNHVKA LGQGLMPLQG TLSESPEALA
     QGITQILAAF RELERVYVYA SLKSDQDTAD AHYQSYAAKA ESLAATISSQ AAFMEPEILA
     IDPAVLNDWL KNPLLVPFAH FITSMISKRD HILSANEEAL LSAASDALNA SRSTFNVLNN
     SDIEFGFVED EDGQAVQLSN GLYGQLIRST NRAVRQEAFE SLYATYGALK NTFATTLAGE
     IKRHNFLASA HHYDSAQLAA LDQNHIPESV YSTLVEQVNA HLPLLHRYVA LRKRLLQVDD
     LHMYDMYTPL TGKPALSYTY EEAQATGKEA LSVLGPDYLS HVEEIFDNRY IDVVENKGKR
     SGAYSGGAYD TNPFILLNWH DSVDELYTLV HETGHSVHSW YTRHNQPYVY GDYPIFVAEI
     ASTTNENLLT AHLLDTQTDP AVRAYILNYY LDGFKGTVFR QTQFAEFEHW IHQQDQEQQP
     LTAETLSNYY GDLNARYYGP QVARDPEIAL EWARIPHFYM NYYVYQYATG FAAASTLAEK
     ILSDDDSATE KYINYLKSGS SEYAIDTMKL AGVDMTKPDY LEAAFAVFEA RLDELESLLE
     TNFDK
//
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