ID   A0A0G1B4A2_9BACT        Unreviewed;       887 AA.
AC   A0A0G1B4A2;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=Peptidase M16 domain protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=UV38_C0003G0231 {ECO:0000313|EMBL:KKS68004.1};
OS   candidate division TM6 bacterium GW2011_GWE2_42_60.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619076 {ECO:0000313|EMBL:KKS68004.1, ECO:0000313|Proteomes:UP000034453};
RN   [1] {ECO:0000313|EMBL:KKS68004.1, ECO:0000313|Proteomes:UP000034453}
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   -!- 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:KKS68004.1}.
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DR   EMBL; LCEG01000003; KKS68004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1B4A2; -.
DR   STRING; 1619076.UV38_C0003G0231; -.
DR   Proteomes; UP000034453; 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; 4.
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; METALLOPROTEASE; 1.
DR   PANTHER; PTHR11851:SF229; PEPTIDASE M16 DOMAIN PROTEIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 2.
DR   Pfam; PF05193; Peptidase_M16_C; 2.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 4.
DR   PROSITE; PS00143; INSULINASE; 1.
PE   3: Inferred from homology;
FT   DOMAIN          32..171
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          180..357
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
FT   DOMAIN          505..632
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          640..818
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   887 AA;  100433 MW;  C242BAB9F8779D49 CRC64;
     MRAFLQILRI ATVIEKIFKH VLKNGLTVLI MPRHQVPKVS LQLWYNVGSK DEESGARGLA
     HLIEHMIFKG TEKLSETDIN IITNKLSGVC NAFTSNDYTG YLFDVPSQHW LEVLPVMADC
     MKNCTFKKEF LNSELKAIIQ ELKMYNDDYL STLIEKMVTS MFPDHPYHYP VIGFKQDLWN
     VSRAQILSFY RRFYGPNNAV LVIVGDVDIE EAFDNIEKAF GSIEPLKTIP KKATYHTFDI
     TNQNVTIYRE VQQPLMLFAW TIPGVSEKKE YLLDLMSWLV GAGRGARLYN RLVTELGIAT
     ELQSFVYDLF DCGIFFIYAQ PRTLEDMPRI KEVILEEIEK LRKGEISDKE IARARRKTDM
     DLLSLPENNQ KLAYMLGKYY LATGDDGFLN QYASYPQENI KADLKELFER YFSPALASSG
     TMLPLSEQDR DLWLLQQETS DAEDARILEG KKRKAPIEGP RYSENITIAP PKKFAYPRAQ
     TFTLSNGLKV FALDRPGSGK IDLILDLKAK HFYDSVEEQG LSMLMTDLLQ EGTTKHSAQE
     LAEEIESLGM ELNTFPGQMS ITMLTEDADK GLELLAEVLM QPAFDKESIE RVRSQMISEL
     KLFWDNPTDF FGQIARQKIY GTHPYSHNMM GTEKTVASLG KKDIKRVYER SITPNGGRIA
     IVGDFGKTDP KTLLQKHLGE WTGAPVKDFD FPSIAPVKHD IVSYPFNRDQ LVLGYGGLSV
     KRLHEDFDAL LLFDQTFTGG VLGSMGSRLF ELREQSGLFY TIGGSILAGS ALQPGMIFIK
     ALVSSDRLFE AEKAIEGVIK KGAQDLTDNE LEEARNALIN SLVDHFAAQK QIAATFLSLD
     TYGFPTDYFD TRPERLLSIK KETVQAAAAR LLDPQKLVKF RVGRIPA
//