ID A0A0A0M7S7_9GAMM Unreviewed; 436 AA.
AC A0A0A0M7S7;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:KGO99023.1};
GN ORFNames=N791_07100 {ECO:0000313|EMBL:KGO99023.1};
OS Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO99023.1, ECO:0000313|Proteomes:UP000030003};
RN [1] {ECO:0000313|EMBL:KGO99023.1, ECO:0000313|Proteomes:UP000030003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO99023.1,
RC ECO:0000313|Proteomes:UP000030003};
RA Wang Q., Wang G.;
RT "Genomic analysis of Lysobacter defluvii.";
RL Submitted (AUG-2013) 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:KGO99023.1}.
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DR EMBL; AVBH01000035; KGO99023.1; -; Genomic_DNA.
DR RefSeq; WP_027070391.1; NZ_AVBH01000035.1.
DR AlphaFoldDB; A0A0A0M7S7; -.
DR STRING; 1385515.GCA_000423325_02390; -.
DR eggNOG; COG1473; Bacteria.
DR OrthoDB; 9777385at2; -.
DR Proteomes; UP000030003; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
DR CDD; cd05667; 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:KGO99023.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030003};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..436
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001966745"
FT DOMAIN 226..322
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 436 AA; 46227 MW; 2EC0083C09533017 CRC64;
MRQLLLPVLL ASLLTPVAAT AQDASGRPEV GAAAERLREE VVALRRHFHQ FPELSNREVE
TSAKVAEHLR ALGLEPRTGI AHHGVVAIIK GGRPGPRVAL RADMDALPVT ERTGLPFASE
VTTTFNGQET GVMHACGHDA HTAILLGVAD ALVAMRDELP GEVMLVFQPA EEGAPPGEEG
GASLMLEEGL FADFRPEAMF GLHVFSSLPV GTIAVRGGPL MAASDRFTIT VQGRQTHGSR
PWGGVDPIVA AADLVGSAQT VVSRRSDLAH QPAVVSFGEF HGGIRYNIIP DQVEMAGTIR
TFDEGMRSKI HADLDNVARH VAAAHGATVT TEIPAGTGNP VTVNDPDLTA RMLPSLRAAA
GVENVIEPPL QMGAEDFAYY AREVPSMFFF VGATSEGIDP ATAPSNHSPE FLLDEASLDV
GLRAMLQVTL DYLEGH
//
