ID   A0A1F6FGV9_9BACT        Unreviewed;       605 AA.
AC   A0A1F6FGV9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Oligoendopeptidase F {ECO:0008006|Google:ProtNLM};
GN   ORFNames=A3G90_03475 {ECO:0000313|EMBL:OGG85095.1};
OS   Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_12_FULL_45_26.
OC   Bacteria; Candidatus Kaiserbacteria.
OX   NCBI_TaxID=1798525 {ECO:0000313|EMBL:OGG85095.1, ECO:0000313|Proteomes:UP000177325};
RN   [1] {ECO:0000313|EMBL:OGG85095.1, ECO:0000313|Proteomes:UP000177325}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU003435};
CC       Note=Binds 1 zinc ion. {ECO:0000256|RuleBase:RU003435};
CC   -!- SIMILARITY: Belongs to the peptidase M3 family.
CC       {ECO:0000256|RuleBase:RU003435}.
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:OGG85095.1}.
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DR   EMBL; MFMM01000001; OGG85095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6FGV9; -.
DR   STRING; 1798525.A3G90_03475; -.
DR   Proteomes; UP000177325; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
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|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          128..181
FT                   /note="Oligopeptidase F N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08439"
FT   DOMAIN          341..585
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   605 AA;  68166 MW;  31A88950721B7A59 CRC64;
     MKKPSLQYTA SPELPKLSNY KTEWDLTVYY KNEKDPKIDK DIEATIAIYK AFAKKWRNKK
     FTTDSKTLKA ALTEYEALAG NPDTSRPGRY FGLRAELNAT DSTADKALAL LRKRLRPAAD
     EILFFTLELG KIPKSAQKSF LKDPALAHFR YLLEQIFRAA AHDLTEAEEK IIRLKAQSSG
     MWQQVTDKLL STSEITWKGK KMPLQEAIVA IDSQKSSDKP KLWKIIIDTL ETFGIVAEHE
     FNAIITDVRT EDDLRNYSKP YSGTAIAYQH DEKSIESFVE AVTKKGFALS KKFYELKAAY
     HGVEAIHYSQ KYDSIGTTSF ISLDEALTVC RDVFYKVNPE YGKVFDGMLV NGQIDVYPKK
     GKSGGAFMSS ETGHPINVML NHTDTMKGLE TIAHEMGHAI HASRSALNTP LYAGHTILTA
     ETASTLFENL VFDALYEVAD TQTKLILLHD KLTGDIATVQ RQIAFFNCEL EIHNTIHSKG
     AMTHGELKEC MYRHLKSYLG KAVEITPEDG VSYIYVGHLR YGFYVYTYAF GHLLSSVMAA
     KYKADNKFST EIDTFLTSGQ SASAVDIYKR IGFDITTPDI FAEALKAQER DITTFKKLLQ
     KQQKA
//