ID A0A031LVJ6_9GAMM Unreviewed; 447 AA.
AC A0A031LVJ6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:EZQ11504.1};
GN ORFNames=CL42_05000 {ECO:0000313|EMBL:EZQ11504.1};
OS Acinetobacter sp. Ver3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=466088 {ECO:0000313|EMBL:EZQ11504.1, ECO:0000313|Proteomes:UP000023816};
RN [1] {ECO:0000313|EMBL:EZQ11504.1, ECO:0000313|Proteomes:UP000023816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ver3 {ECO:0000313|EMBL:EZQ11504.1,
RC ECO:0000313|Proteomes:UP000023816};
RA Kurth D.G., Ordonez O.F., Albarracin V.H., Revale S., Farias M.E.;
RT "Polyextremophylic features in the genome of Acinetobacter sp. Ver3
RT isolated from a high altitude andean lake.";
RL Submitted (MAR-2014) 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:EZQ11504.1}.
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DR EMBL; JFYL01000010; EZQ11504.1; -; Genomic_DNA.
DR RefSeq; WP_051586524.1; NZ_JFYL01000010.1.
DR AlphaFoldDB; A0A031LVJ6; -.
DR eggNOG; COG1473; Bacteria.
DR Proteomes; UP000023816; 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 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:EZQ11504.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..447
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001558245"
FT DOMAIN 228..324
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 447 AA; 48651 MW; 8FCEE60398FC7CBE CRC64;
MISLRLFFAC TILPLCSTLS FADWVDDGVN AVEQHTIKLR QHIHQHPELG NMEFKTSALV
QKELKKYGIE VRTGYAKTGV IGILKGAKPG PVMALRADMD ALPIEEKTGL SFASKAKAIY
QGKETPVMHA CGHDAHTAML LGAAKVLSEN KDKIAGTVVF VFQPAEEGGA DIDNFSHGDQ
IGSRKMIADG ALKNPKPEVI FGMHVMAGMP SGHIFYKDGT ILNSADHLRI QVSGKQVHGS
MPWLGRDPIY ASSQMISNMQ SLISRRADLT KGMGAISIGS IQGGTVGNVI PEQVNMVGTI
RSNNEEVRQN ILKDLPKLIE HNAHANDVKA KVEIAAYAPV TTNDKTLTQL IAPSLAKVHG
EDKLHVLENN ASASEDFAYY GQLMPSLFIF IGATPQDQEI SKAAPNHNPK FIVDDATLKT
GVESHIRFVM DYPTIAQQVK QDWNNKS
//
