ID   A0A0Q7D917_9CAUL        Unreviewed;       452 AA.
AC   A0A0Q7D917;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=Peptidase M20 {ECO:0000313|EMBL:KQW68266.1};
GN   ORFNames=ASC73_17295 {ECO:0000313|EMBL:KQW68266.1};
OS   Phenylobacterium sp. Root1277.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Phenylobacterium.
OX   NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW68266.1, ECO:0000313|Proteomes:UP000051150};
RN   [1] {ECO:0000313|EMBL:KQW68266.1, ECO:0000313|Proteomes:UP000051150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1277 {ECO:0000313|EMBL:KQW68266.1,
RC   ECO:0000313|Proteomes:UP000051150};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQW68266.1, ECO:0000313|Proteomes:UP000051150}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root1277 {ECO:0000313|EMBL:KQW68266.1,
RC   ECO:0000313|Proteomes:UP000051150};
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:KQW68266.1}.
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DR   EMBL; LMDZ01000007; KQW68266.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q7D917; -.
DR   Proteomes; UP000051150; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051150};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           36..452
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006304931"
FT   DOMAIN          235..331
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   452 AA;  47180 MW;  1E88AF52127C7999 CRC64;
     MPATGGAAHR ANKTMTFALL LPAAAVLLGA TVASAAPFDV PAARDSVTAA FEKDRSRLEA
     LYMDLHAHPE LGFQETRTAA RLAKEMKALG LDVTEGVGGT GVVAVLRNGA GPTVLVRTEL
     DALPMKEETG LPYASKVTAQ WEGRETFVAH SCGHDMHMAA WVGAARALVA QKARWRGTVL
     FVAQPSEETV SGARAMIADR FFERFGKPDY GFALHVGPGL AGGVYYKPGV LSSNSDALEL
     TFTGRGGHGS MPHATIDPVL MASRFVVDVQ SIVSREKDPA AFGVVTIGAI QAGSAGNIIP
     ETAQLKGTIR TYDAGVRQKI LDGVTRVAKA QADMSAAPPP KLEFIPGGKA VVNDAALTAT
     TADVFKQAFG SMAVEIPQPG SASEDYSEFI LAGVPSVYFA IGSYTPETMK AAAGKPLPVN
     HSPMFAPAIQ PTLQTGVTAM ALAVMNVLPV EP
//