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Database: UniProt
Entry: A0A0Q4YBU2_9BURK
LinkDB: A0A0Q4YBU2_9BURK
Original site: A0A0Q4YBU2_9BURK 
ID   A0A0Q4YBU2_9BURK        Unreviewed;       407 AA.
AC   A0A0Q4YBU2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Amidohydrolase {ECO:0000313|EMBL:KQP23267.1};
GN   ORFNames=ASF43_05185 {ECO:0000313|EMBL:KQP23267.1};
OS   Pseudorhodoferax sp. Leaf267.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae.
OX   NCBI_TaxID=1736316 {ECO:0000313|EMBL:KQP23267.1, ECO:0000313|Proteomes:UP000051560};
RN   [1] {ECO:0000313|EMBL:KQP23267.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23267.1,
RC   ECO:0000313|Proteomes:UP000051560};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP23267.1, ECO:0000313|Proteomes:UP000051560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf267 {ECO:0000313|EMBL:KQP23267.1,
RC   ECO:0000313|Proteomes:UP000051560};
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:KQP23267.1}.
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DR   EMBL; LMMV01000001; KQP23267.1; -; Genomic_DNA.
DR   RefSeq; WP_056177360.1; NZ_LMMV01000001.1.
DR   AlphaFoldDB; A0A0Q4YBU2; -.
DR   STRING; 1736316.ASF43_05185; -.
DR   OrthoDB; 8875216at2; -.
DR   Proteomes; UP000051560; 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:KQP23267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051560}.
FT   DOMAIN          198..293
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   407 AA;  43407 MW;  20D92EA20F2F5407 CRC64;
     MLAPVLRAGG RAFAHIARFH PELTALRRDL HAHPELGFEE FYTADRIADA LRLCGVDEVH
     TGIAKTGVVG VIRGRSTASG GMLGLRADMD ALPMVEQGDR DWRSARNGLM HGCGHDGHTA
     MLVGAARYLA ETRRFDGTAV LIFQPGEEGF AGARAMIEDG LFQRFPVDSV YAMHNWPGME
     PGTVGLNSGA MMAAADRITI TITGKGGHGA HAYQTVDPVL VAAHIITAAQ SIVSRNTRPI
     DAAVVSLCAM QAGDLGAMSV VPGEATLVGT VRTFDAKVQA MVERRLAELC SAIAQGFGAS
     AAVRFERIYP ATINTREQAR FAGDVAERLV GAERLVRDME PSMGAEDFSF MLQARPGAYL
     RIGQGAPDGC YLHNSRYDFN DEILPLGAAL HAGLVEQGMP LADPQSD
//
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