ID   A0A0G0JS82_9BACT        Unreviewed;       420 AA.
AC   A0A0G0JS82;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Processing protease {ECO:0000313|EMBL:KKQ65985.1};
GN   ORFNames=US86_C0007G0030 {ECO:0000313|EMBL:KKQ65985.1};
OS   Candidatus Daviesbacteria bacterium GW2011_GWA2_38_24.
OC   Bacteria; Candidatus Daviesbacteria.
OX   NCBI_TaxID=1618422 {ECO:0000313|EMBL:KKQ65985.1, ECO:0000313|Proteomes:UP000034235};
RN   [1] {ECO:0000313|EMBL:KKQ65985.1, ECO:0000313|Proteomes:UP000034235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M16 family.
CC       {ECO:0000256|ARBA:ARBA00007261, ECO:0000256|RuleBase:RU004447}.
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:KKQ65985.1}.
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DR   EMBL; LBUP01000007; KKQ65985.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0JS82; -.
DR   PATRIC; fig|1618422.5.peg.936; -.
DR   Proteomes; UP000034235; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.830.10; Metalloenzyme, LuxS/M16 peptidase-like; 2.
DR   InterPro; IPR011249; Metalloenz_LuxS/M16.
DR   InterPro; IPR011765; Pept_M16_N.
DR   InterPro; IPR001431; Pept_M16_Zn_BS.
DR   InterPro; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR11851:SF149; GH01077P; 1.
DR   PANTHER; PTHR11851; METALLOPROTEASE; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Hydrolase {ECO:0000313|EMBL:KKQ65985.1};
KW   Protease {ECO:0000313|EMBL:KKQ65985.1}.
FT   DOMAIN          14..154
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..340
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   COILED          308..342
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   420 AA;  48012 MW;  E5A032D7240EA715 CRC64;
     MYKIKTLPNG LTLITIHIPT LESVTTLLAV GAGSRYEARN INGISHFLEH MFFKGSKKYP
     SAEQIATMVD SIGAINNAAT DKEVTLYWIK SASKHIELSS DILSSMLKEP LLESDEIEKE
     KGVIVEELRM FKDMPARYVW DLYENLQFGD QPLGWDIGGD EKTVMDLKRD DFLNYMNSLY
     KAENMALVYV GNLPENIEEL AIKYFADLQR GAKNSFKPYH WEEQKEPRVN IYYKKTDQVN
     LILGVEGYDR EDDRRYAARV LGIILGEGMS SRLFNEIRMK RGFAYHVSAG HSSYHDTGNF
     AVFGGLKLEK VKEALKVILE QLEKASKEVV SLDELKKAKE MERGRVALRS ESTNFLAEHF
     GVKFVLDREL ETFDEYLAKI DAVTAEEVKQ VAIDLFQSKK FNLQIIGPLE NTDEFKLLLK
//