ID   A0A0G0J9M0_9BACT        Unreviewed;       466 AA.
AC   A0A0G0J9M0;
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=Acetylornithine deacetylase/succinyl-diaminopimelate desuccinylase-like protein {ECO:0000313|EMBL:KKQ24856.1};
GN   ORFNames=US39_C0013G0026 {ECO:0000313|EMBL:KKQ24856.1};
OS   Microgenomates group bacterium GW2011_GWC1_37_12b.
OC   Bacteria.
OX   NCBI_TaxID=1618510 {ECO:0000313|EMBL:KKQ24856.1, ECO:0000313|Proteomes:UP000034251};
RN   [1] {ECO:0000313|EMBL:KKQ24856.1, ECO:0000313|Proteomes:UP000034251}
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   -!- 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:KKQ24856.1}.
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DR   EMBL; LBSU01000013; KKQ24856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0J9M0; -.
DR   STRING; 1618510.US39_C0013G0026; -.
DR   Proteomes; UP000034251; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 2.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR041657; HTH_17.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   InterPro; IPR010093; SinI_DNA-bd.
DR   NCBIfam; TIGR01764; excise; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 1.
DR   Pfam; PF12728; HTH_17; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   4: Predicted;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          5..50
FT                   /note="Helix-turn-helix"
FT                   /evidence="ECO:0000259|Pfam:PF12728"
FT   DOMAIN          238..346
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   466 AA;  51890 MW;  F6D29EA62BB2F500 CRC64;
     MDTKYTIAEA AKITKVSQRT LLRAIKNGNL KTEKAGRRHL ISERTLNSYL GGSNISLNDA
     LLTFLKNKKS EMVATLQKIV SMPSISSEIG QEEKLANYIK KRLDEWGIRC VVYKEGTSIA
     VRATYGFANE GFLLDSPLDT LPAGDSVKWT HPPFDGEVVN GKMYGRGTAD AKAGIVTQLY
     SLLFFKRNID EDKVRIELVF DGGEQDGEFL GMKQVIGRGL HVKAGLIGYS GDLEELMYGA
     RGYHRYEFEV NGKAVHTGSR YKKGVNAISN MVKFIESVEA QELPRSKNKL FPFGARLTFS
     IISGGRAINM IPDSCISKLD VRTIPEMKKK DVDEIIIKHI TRLKKKNPEF DVNFRYLTGQ
     EAYAISENDN LIKSLDFAVK RSMGSTLKHT ASGPAHVGNL LFECGISTAV WGPKGENAHS
     YDEYIEIDSL TKTVDIYVRT IAKYFDIDDS AVITNPSANY DVSDWS
//