ID   A0A140L4E2_9CLOT        Unreviewed;       630 AA.
AC   A0A140L4E2;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Oligoendopeptidase F {ECO:0000256|RuleBase:RU368091};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU368091};
GN   Name=pepF1_1 {ECO:0000313|EMBL:KXG75417.1};
GN   ORFNames=AN619_16810 {ECO:0000313|EMBL:KXG75417.1};
OS   Thermotalea metallivorans.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Thermotalea.
OX   NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG75417.1, ECO:0000313|Proteomes:UP000070456};
RN   [1] {ECO:0000313|EMBL:KXG75417.1, ECO:0000313|Proteomes:UP000070456}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B2-1 {ECO:0000313|EMBL:KXG75417.1,
RC   ECO:0000313|Proteomes:UP000070456};
RA   Patel B.K.;
RT   "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT   isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL   Submitted (DEC-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:KXG75417.1}.
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DR   EMBL; LOEE01000034; KXG75417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A140L4E2; -.
DR   STRING; 520762.AN619_16810; -.
DR   PATRIC; fig|520762.4.peg.1866; -.
DR   Proteomes; UP000070456; 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:UP000070456};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU368091}.
FT   DOMAIN          146..215
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          236..616
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   630 AA;  73416 MW;  FA93513FFA146216 CRC64;
     MGYNKEKNIM MKSRNQERRM WFLPRQGNMN RNKKNIPKRS EVPFQWKWKL EQIYETDKHW
     EKDFSAIESM LEDIEKYVGK LGNSSQCLYE ALNLSDHISR KLENVFIYAK MRKDEDNTVS
     KYQAMTDRAQ SLSVAVHSRL SFMVPEILSI PEDRIKGFLK ENEKLTLYTF YLEEILRQKS
     HVLSKEEEQI LAQVGELAAA PKNIFGMINN ADIKFPTIRD EKGEEIEVTK GRYVKLLESE
     DRRVRRDAFR ALYSSYEKQK NTIAATLNYS VKKDVFYARV RKYESSLQAS LDGDNIPLSV
     YDNLIEAVHG HLDSMYRYMA LRKKALGIDE LHMYDLYTPM VKAVKMHIPY QEAKQKVKLG
     LAPLGEEYVS LLEKGFTEGW IDVYENEGKT SGAYSWGSYD SPPFVLLNYQ DSIHDLFTLA
     HEMGHSLHTY YANHHQPYPY AGYKIFVAEV ASTVNEALLM EYLLNHIKEE NMRMYLLNHY
     LEQFRTTLYR QTMFAEFEKI IHEKVEKGEP LTPELLCEVY GELNRKYYGP EVMIDDEIKM
     EWARIPHFYN AFYVYKYATG FSAAISLSQQ ILKEGAPAVD RYIGFLKKGG SDYPIALLKG
     AGVDMTTAAP MHDALEVFEK LLNELEKGLQ
//