ID   A0A0G1QNC9_9BACT        Unreviewed;       413 AA.
AC   A0A0G1QNC9;
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=Processing protease {ECO:0000313|EMBL:KKU46521.1};
GN   ORFNames=UX62_C0012G0007 {ECO:0000313|EMBL:KKU46521.1};
OS   Microgenomates group bacterium GW2011_GWA2_46_7.
OC   Bacteria.
OX   NCBI_TaxID=1618502 {ECO:0000313|EMBL:KKU46521.1, ECO:0000313|Proteomes:UP000034318};
RN   [1] {ECO:0000313|EMBL:KKU46521.1, ECO:0000313|Proteomes:UP000034318}
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:KKU46521.1}.
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DR   EMBL; LCMX01000012; KKU46521.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G1QNC9; -.
DR   PATRIC; fig|1618502.3.peg.203; -.
DR   Proteomes; UP000034318; 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:UniProtKB-KW.
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;
KW   Hydrolase {ECO:0000313|EMBL:KKU46521.1};
KW   Protease {ECO:0000313|EMBL:KKU46521.1}.
FT   DOMAIN          15..163
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          171..342
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   413 AA;  45957 MW;  70FA1622A4BD8372 CRC64;
     MKFDVSYSKL KNGVRVLTVP IPGVESVTAM ILVKTGSRNE DLKQAGISHV LEHMVFKGTS
     KYPSPMHIAE AVDSIGGEQN AFTSKEYTGY YITSAAKHLG LTLDIQAEML TKPLLPQVDL
     EREREVIVEE INMYEDQPMA MAGELFENLM YDGSSMGRLI IGTKETVRGT NAEDLRQYMG
     EWYRGGNMLV VVAGKIANHQ FSNSQIEEQF GEMSEGPITG YKTVATFGQP EAQHHKKKTE
     QAHFVIGVPA LPMTDPRRYA LSIAQVVLGG NMSSRLFNEI REKRGLAYYV RADLDTSYDC
     GYLAVRSGVK LTKLKEAMEI VRAEMLKLGE TMTQSELKRG QDYLLGKMPL SLEDSMGVAQ
     FFGTRTLILN EIRQPTDVEQ AIKAVKIEEV RGILTDLVKE ELIRSVVVGP KAS
//