ID   A0A2A4Z9Q2_9PROT        Unreviewed;       430 AA.
AC   A0A2A4Z9Q2;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Peptidase M16 {ECO:0000313|EMBL:PCJ03510.1};
GN   ORFNames=COB13_02490 {ECO:0000313|EMBL:PCJ03510.1};
OS   OCS116 cluster bacterium.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; OCS116 cluster.
OX   NCBI_TaxID=2030921 {ECO:0000313|EMBL:PCJ03510.1, ECO:0000313|Proteomes:UP000218076};
RN   [1] {ECO:0000313|Proteomes:UP000218076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Wheat C.G., Glazer B.T., Huber J.A.;
RT   "A dynamic microbial community with high functional redundancy inhabits the
RT   cold, oxic subseafloor aquifer.";
RL   Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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:PCJ03510.1}.
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DR   EMBL; NVUS01000002; PCJ03510.1; -; Genomic_DNA.
DR   Proteomes; UP000218076; 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          27..170
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          177..347
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   430 AA;  47546 MW;  D1F4AA129519D07F CRC64;
     MNDVSQTIEI EPGVHSTRLD NGLTIVTHQM PLQSIAXGAW IKAGSRNEDL AEHGVAHFLE
     HMAFKGTKNR TAKQIVEQIE NVGGDMNAAT GIEVTSYYFR LLKDDLALGL EILADILLNP
     LFETEEMDKE KQVILQEIAA TDDDADDVLY DKLIENAYAE QAIGRSILGT PDSVMALTKD
     QLSGFLAKHY VPENMIIAMA GGASHGQVLE LVKKYFGTMP AQKPATLPAA KFTADNVMIE
     KSLEQNYLVL GFESFHFNHP DFFAQQILSQ LFGGGMSSRL FQNIREQKGL CYSIYSGSWG
     FDDTGLIFIY AATNADNIPI VKDLIYKELI DLLADISPAE LQRACNQIKA GQMMSLESPV
     SRSEQIARQS IFYKNLIKID DIINRLEAVT LADLKRVAKD LFLHAPAQKL SNDALQLSDL
     KPHITVQVGG
//