ID   A0A0M1P819_9BACL        Unreviewed;       596 AA.
AC   A0A0M1P819;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   ORFNames=AM231_15880 {ECO:0000313|EMBL:KOR90460.1};
OS   Paenibacillus solani.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1705565 {ECO:0000313|EMBL:KOR90460.1, ECO:0000313|Proteomes:UP000036932};
RN   [1] {ECO:0000313|Proteomes:UP000036932}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-22460 {ECO:0000313|Proteomes:UP000036932};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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:KOR90460.1}.
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DR   EMBL; LIUT01000001; KOR90460.1; -; Genomic_DNA.
DR   RefSeq; WP_054403388.1; NZ_LIUT01000001.1.
DR   AlphaFoldDB; A0A0M1P819; -.
DR   PATRIC; fig|1705565.3.peg.5258; -.
DR   OrthoDB; 9766487at2; -.
DR   Proteomes; UP000036932; 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:UP000036932};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          113..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          202..582
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  68696 MW;  D642DDB4818D9819 CRC64;
     MEQLLKRADV PKEHQWKLED MFADQKAWDE SFAELKNLLK RAGDYQGKLD NAASIKACFE
     LEDEISYNAE RLYVYAHMHH DEDTANPTYQ ALSAKAKKLN VEAGEALSFI TPEILSLSEA
     ELDKLIDDPA LQDFKFTLTE MKREKAHVLS KTEEALLAQV GNLSSAPQTI FGMLNNADMK
     FPKITNEDGK EVELTHGNYI QFLESPNREV RERAFKAVYE TYGKQKNTIA ATLNANINKN
     IFYSRVRKYP SVLEMALYGD NIPKEVYTNL IDTIHESLPL LHRYMELRKK LLGVDELHMY
     DLFAPLVEEY KWDITYEEAK QMTKEGLTPL GDDYLNSLQE GYDNGWIDVY ENENKRTGAY
     SWGAYGTHPY VLLNHKDNLN SMFTLAHEMG HALHSYYSDN ALKYRDAQYT IFLAEVASTT
     NEALLMDYLL KNAKDPKQKM YLLTYYADQF RTTVFRQTMF AEFEKIVHER AESGESLTAQ
     DLSDIYYELN VKYHGKGMQV DKEIGMEWAR IPHFYNSFYV YKYATGFSAA TSFSKQILEE
     GQPAVDRYLG FLKSGGSDYS INILKKAGVD MSSPEPIREA MSVFEDIIRQ MEQLTK
//