ID   A0A0G1CC91_9BACT        Unreviewed;       424 AA.
AC   A0A0G1CC91;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:KKS83039.1};
GN   ORFNames=UV58_C0002G0049 {ECO:0000313|EMBL:KKS83039.1};
OS   Candidatus Wolfebacteria bacterium GW2011_GWC1_43_10.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1619011 {ECO:0000313|EMBL:KKS83039.1, ECO:0000313|Proteomes:UP000034810};
RN   [1] {ECO:0000313|EMBL:KKS83039.1, ECO:0000313|Proteomes:UP000034810}
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:KKS83039.1}.
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DR   EMBL; LCFA01000002; KKS83039.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1CC91; -.
DR   Proteomes; UP000034810; 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          16..164
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          169..343
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   424 AA;  47643 MW;  4CCF743CF5B945D5 CRC64;
     MSLNANKFVL KNGLRVLVIP QKESPSVTVG IFVEAGAAYE NRQNNGLSHF LEHMCFKGTQ
     TRPRPMDISS EMESLGASYN AFTSRDLTGY WAKVAYTKLD KIFDILADMY LNPVFNEKEI
     EKEKGVIVEE INMYEDQPRT KVSETLDALM YGNQPAGWSI AGPKENIRKI DRNDFLKYRS
     AHYHGAKTVV VIAGRIDSKK AKALVEKYFS KIKKDKKIAP VKTSESQKSS ALALVKRDLD
     QTHFILGLKA FSSSSPKKYP LVLLSEILGG GMSSRLFQKI REELGAAYYV GSSPSLFLTH
     GYLEIFAGVN HQKSIVAIKA VLEELRKILK KGVEIKELKR VKDHFLGTFL LSLETSSDLA
     FFYGEQETVL GKIQSPENVI KKISLVTQKD IQKIAKEVFD NRKLNLAVIG PYENGSDFKK
     ILKI
//