ID   A0A0G1P8Q7_9BACT        Unreviewed;       421 AA.
AC   A0A0G1P8Q7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   SubName: Full=Peptidase, M16 family {ECO:0000313|EMBL:KKT92684.1};
GN   ORFNames=UW91_C0017G0012 {ECO:0000313|EMBL:KKT92684.1};
OS   Parcubacteria group bacterium GW2011_GWF2_45_11.
OC   Bacteria.
OX   NCBI_TaxID=1618973 {ECO:0000313|EMBL:KKT92684.1, ECO:0000313|Proteomes:UP000034898};
RN   [1] {ECO:0000313|EMBL:KKT92684.1, ECO:0000313|Proteomes:UP000034898}
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:KKT92684.1}.
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DR   EMBL; LCKE01000017; KKT92684.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1P8Q7; -.
DR   PATRIC; fig|1618973.3.peg.539; -.
DR   Proteomes; UP000034898; 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:InterPro.
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;
FT   DOMAIN          14..161
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          167..341
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   421 AA;  46938 MW;  34215BC665ABEF61 CRC64;
     MYKLETLANK TKILLAPQKA TDAVTILALV KVGSRHEAAP VNGISHFIEH LLFKGTTSRP
     TSLDISKELD GVGADFNAFT GKDHTGYYVK VSHDKLALAL NIVSDMLFNS LFDQQEIAKE
     RGVIIEEINM YDDNPLISIG NLFEEVIFKG SSLGNDIAGP KKNIREISRR QITDYFWNHY
     RSDNILVGVG GNFDLASARR LIKKYFSAPG GNVKKSRFKK FAAAQTKLRI KVKYKATEQV
     QVALGFPAYR AGDPRNYGLT LLSVILGGNM SSRLFIEIRE KLGLAYHIRS GIITYEDTGA
     LEVFAGLDKA KVALALKTIR RELESFAQGQ ITDDELRRAK EFVKGKLTLS LEDSAAHIQW
     LAEQQLLQGR IETLAVKLKK IDQVSVKQIK KVALEVIKKN KYNVAVIGPY RSASSFLNIF
     K
//