ID   A0A0G0KHD5_9BACT        Unreviewed;       422 AA.
AC   A0A0G0KHD5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:KKQ78152.1};
GN   ORFNames=UT00_C0001G0037 {ECO:0000313|EMBL:KKQ78152.1};
OS   Parcubacteria group bacterium GW2011_GWA1_38_7.
OC   Bacteria.
OX   NCBI_TaxID=1618783 {ECO:0000313|EMBL:KKQ78152.1, ECO:0000313|Proteomes:UP000034610};
RN   [1] {ECO:0000313|EMBL:KKQ78152.1, ECO:0000313|Proteomes:UP000034610}
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:KKQ78152.1}.
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DR   EMBL; LBVD01000001; KKQ78152.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0KHD5; -.
DR   Proteomes; UP000034610; 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          20..161
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          168..341
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   422 AA;  47664 MW;  DDD323CC5D744262 CRC64;
     MNYKKKVLKN GLRVIAVPMK ASPSVTVMSL IEAGSKYENK QNNGISHFLE HMCFKGTEKR
     LKAIDISREF DAMGAQNNAF TSQEVTGYWA KASNKHTDQI LDIISDMYLR PTFPVADLET
     EKGVIVEEIN MYEDLPNRLV HEVFDELLYG DQPAGWSVAG TRENVRGFER DDFVNYRKNH
     YVASATTVVV AGDIDPALIF KKVSKAFDGM PVTKKVGKKK VVEKQNGPMV KLRFKETDQT
     HLVIGFRAYD LYDKKTQALR ILSVVLGNGM SSRLFQKMRE ELGICYYVRS AVDGLTDHGT
     FLISAGVDSS RVEEGVKGIL DEVKKIKSEK VPESELRKAK DYLIGNMYLG LESSDAQANF
     FGSQEIMKEK IKTPKEVEKE IQKITAKDIS KVAKEIITND RLNMAIVGKY KDESRFKKIL
     KI
//