ID   A0A0Q7T842_9CAUL        Unreviewed;       416 AA.
AC   A0A0Q7T842;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Acetylornithine deacetylase {ECO:0000313|EMBL:KQY96742.1};
GN   ORFNames=ASD25_01880 {ECO:0000313|EMBL:KQY96742.1};
OS   Brevundimonas sp. Root1423.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=1736462 {ECO:0000313|EMBL:KQY96742.1, ECO:0000313|Proteomes:UP000051815};
RN   [1] {ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|Proteomes:UP000051815};
RA   Garrido-Oter R., Bai Y.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY96742.1, ECO:0000313|Proteomes:UP000051815}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1423 {ECO:0000313|EMBL:KQY96742.1,
RC   ECO:0000313|Proteomes:UP000051815};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQY96742.1}.
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DR   EMBL; LMFL01000001; KQY96742.1; -; Genomic_DNA.
DR   RefSeq; WP_056614875.1; NZ_LMFL01000001.1.
DR   AlphaFoldDB; A0A0Q7T842; -.
DR   Proteomes; UP000051815; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03885; M20_CPDG2; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051815}.
FT   DOMAIN          201..297
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   416 AA;  43278 MW;  C952769A03841C4E CRC64;
     MRIQPSDQLV LNHVAAREDI IVGRAIDWAG VNSGSRNTGG LAIMLDRLEA EARYLPAVVE
     RVPTGASTSA GDDGVVRTEV HADALRITAR PLAPIQIVLT GHYDTVFPAD SSFQTVSTRP
     DGALNGPGIA DMKGGISVML AALEAFETHP DREQVGWTVL LSPDEEIGSP ASAPLLAELG
     ARGHIGMTYE PALADGTLAG ARKGSGNYHL IVSGKAAHAG RAFHEGANAV AGAAILATRL
     HALNGQREGV TVNVAKISGG GALNVVADNA IVRFNVRVPD KAASDWIEAA VRDIASDLPF
     PGLVLHLLGG MTRAPKPMDA SQTALFEAVR DTGALLGQTI AWKPSGGVCE GNNLHAAGLP
     NIDTLGVLGG DIHSGQEFAW PASFVERAQL SALILCKIAS SEIDALKLKS LRLETM
//