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Database: UniProt
Entry: A0A0S9MYG5_9BURK
LinkDB: A0A0S9MYG5_9BURK
Original site: A0A0S9MYG5_9BURK 
ID   A0A0S9MYG5_9BURK        Unreviewed;       400 AA.
AC   A0A0S9MYG5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQP38086.1};
GN   ORFNames=ASF44_12795 {ECO:0000313|EMBL:KQP38086.1};
OS   Pseudorhodoferax sp. Leaf274.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736318 {ECO:0000313|EMBL:KQP38086.1, ECO:0000313|Proteomes:UP000051759};
RN   [1] {ECO:0000313|EMBL:KQP38086.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38086.1,
RC   ECO:0000313|Proteomes:UP000051759};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP38086.1, ECO:0000313|Proteomes:UP000051759}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf274 {ECO:0000313|EMBL:KQP38086.1,
RC   ECO:0000313|Proteomes:UP000051759};
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:KQP38086.1}.
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DR   EMBL; LMNA01000026; KQP38086.1; -; Genomic_DNA.
DR   RefSeq; WP_056901388.1; NZ_LMNA01000026.1.
DR   AlphaFoldDB; A0A0S9MYG5; -.
DR   STRING; 1736318.ASF44_12795; -.
DR   OrthoDB; 8875216at2; -.
DR   Proteomes; UP000051759; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd05666; M20_Acy1-like; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017439; Amidohydrolase.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01891; amidohydrolases; 1.
DR   PANTHER; PTHR11014:SF63; METALLOPEPTIDASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G09600)-RELATED; 1.
DR   PANTHER; PTHR11014; PEPTIDASE M20 FAMILY MEMBER; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF005962; Pept_M20D_amidohydro; 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, ECO:0000313|EMBL:KQP38086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051759}.
FT   DOMAIN          186..282
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   400 AA;  43600 MW;  D41E215B28E97F1F CRC64;
     MPILDAFADT GRFRTLRRDI HAHPELGFEE HRTSEIVAGL LAEWGIEVHR GIAGTGLVGV
     LRGSWPDNGK TIGLRADMDA LPLQEVNGFD HRSRHDGRMH ACGHDGHTTM LLAAAWQLAQ
     RRDFAGTVHF IFQPAEEMGK AGARKMIDEG LFERFPCDAV FALHNFNLGR VGNFALNHGA
     LMASSNTWRI TVRGRGTHAS MPHTGLDPVG AVLEIAQALR SLVARTIPST ERALLAVTQI
     QGSDAPNVIP DTAWVGGTVR TFSVDALDKI EARLRHLAGH IAQAHECTAE VMFRRASPPV
     VNHPAEARFA AEVMREIVGD ALVDENLPGV LGAEDFAHML MERPGCYAFL GNGDGDHRMA
     GHGPGPCIIH NTSFDFNDDI IPVGASYFVR LAERWLATPR
//
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