ID   A0A1F8TGX8_9CHLR        Unreviewed;       596 AA.
AC   A0A1F8TGX8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Oligoendopeptidase F {ECO:0000313|EMBL:OGO71217.1};
GN   ORFNames=A2Z37_07260 {ECO:0000313|EMBL:OGO71217.1};
OS   Chloroflexi bacterium RBG_19FT_COMBO_62_14.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1797671 {ECO:0000313|EMBL:OGO71217.1, ECO:0000313|Proteomes:UP000176680};
RN   [1] {ECO:0000313|EMBL:OGO71217.1, ECO:0000313|Proteomes:UP000176680}
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:OGO71217.1}.
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DR   EMBL; MGOM01000035; OGO71217.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8TGX8; -.
DR   Proteomes; UP000176680; 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   CDD; cd09610; 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   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   PANTHER; PTHR11804:SF5; OLIGOENDOPEPTIDASE F; 1.
DR   PANTHER; PTHR11804; PROTEASE M3 THIMET OLIGOPEPTIDASE-RELATED; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU003435};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU003435};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU003435};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU003435};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU003435}.
FT   DOMAIN          199..576
FT                   /note="Peptidase M3A/M3B catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF01432"
SQ   SEQUENCE   596 AA;  68050 MW;  2891039982D1142C CRC64;
     MATLTYKQER WSLEELFPAI ESPALTAGLE KVEGLATAFE SQRRVLQPEM DQREFTRVLQ
     GYDELILEMQ RIEYFAFLLF SEDTQDQKAQ SFMARMQQLA AEMENRTLFF KLWWKALEEP
     QAERLAAGAG DLRYWLEFLR LTKDFTLSEP EEKVINLKDV NGSAAMVTLY DSITNRYSFR
     LEVDGEVKEL TRGELMVYVR NADLALRAAA YQEQLRVFGQ DGPILGQIYQ ALVRDWRSEN
     MDLRGHKSPM SVRNLGNHLP DAVVDTLLEV CRQNAAVFRR YFKLKARWLG TEKLRRYDIY
     APVTAGEKNY TFNAAVELTL ASFDHFDPKI SELARRVFDE HHLDSEVRKG KRGGAFCATV
     TPALTPWVLS SFQGRPDDVA TLAHELGHAV HSMLASHHSV LTQSASLPLA ETASTFGEML
     LVDRLLASDP DPGLQRDLLF RQMDDAYATI MRQAFFALYE RTAHEMIRAG SSVDDLSAAY
     LENLREQFGD SLDLGDDFRH EWVAIPHIFH TPFYVYAYAF GQLLVFSLYK QYRQEGDSFK
     PRYLKLLAAG GSQAPEKILS DAGVDMRSVE FWQGGFQIVA ETLERLEALE VPLKSS
//