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Database: UniProt
Entry: A0A0G0AHH4_9BACT
LinkDB: A0A0G0AHH4_9BACT
Original site: A0A0G0AHH4_9BACT 
ID   A0A0G0AHH4_9BACT        Unreviewed;       416 AA.
AC   A0A0G0AHH4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Peptidase M16 domain protein {ECO:0000313|EMBL:KKP55978.1};
GN   ORFNames=UR50_C0011G0006 {ECO:0000313|EMBL:KKP55978.1};
OS   Parcubacteria group bacterium GW2011_GWC1_34_10.
OC   Bacteria.
OX   NCBI_TaxID=1618891 {ECO:0000313|EMBL:KKP55978.1, ECO:0000313|Proteomes:UP000034499};
RN   [1] {ECO:0000313|EMBL:KKP55978.1, ECO:0000313|Proteomes:UP000034499}
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}.
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:KKP55978.1}.
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DR   EMBL; LBPL01000011; KKP55978.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0AHH4; -.
DR   STRING; 1618891.UR50_C0011G0006; -.
DR   Proteomes; UP000034499; Unassembled WGS sequence.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
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; IPR007863; Peptidase_M16_C.
DR   PANTHER; PTHR43690:SF18; INSULIN-DEGRADING ENZYME-RELATED; 1.
DR   PANTHER; PTHR43690; NARDILYSIN; 1.
DR   Pfam; PF00675; Peptidase_M16; 1.
DR   Pfam; PF05193; Peptidase_M16_C; 1.
DR   SUPFAM; SSF63411; LuxS/MPP-like metallohydrolase; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          32..135
FT                   /note="Peptidase M16 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00675"
FT   DOMAIN          175..321
FT                   /note="Peptidase M16 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05193"
SQ   SEQUENCE   416 AA;  47761 MW;  73232F0400751C6F CRC64;
     MYDPYADFVK HVLANGLEVH SVSWDRPWIG MEIVVHSGGR EDPVTIPGLA HFVEHTVSQN
     IPNREFDPVK EFFEVCGGRA EFGSTSYLST RYKFSIPADL ATFREALDIF GSMLLQAKIK
     KDVERERKVI MREFNQRYPF LDKLEWDMGI RRELFKGHRL ETWNRPLGRP EGFLSITETD
     LQGFYDQHYV PANMSLVFIG GLSIDQVIAE LERSPFGTKK DGRRNAIPQL LSCLPIPAEQ
     TKTVKLSDHV SFKVDQTEYK ATWAFPAHFP NQACRVFDQV LCKILFDEIR EQRGLAYSIG
     TDYADFQDVY EYVIGGRICP EATLYIDDLV RKCIEMVPTR RDMFDRKLKS LKQKCLMIDL
     AGQGLAGNSA ADLASDHRII PMQEVWDELH KVTFEQMSEA TSFLGSDHQY TFITCP
//
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