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Database: UniProt
Entry: A0A1A7RBX7_9GAMM
LinkDB: A0A1A7RBX7_9GAMM
Original site: A0A1A7RBX7_9GAMM 
ID   A0A1A7RBX7_9GAMM        Unreviewed;       449 AA.
AC   A0A1A7RBX7;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   SubName: Full=N-acyl-L-amino acid amidohydrolase {ECO:0000313|EMBL:OBX28207.1};
GN   ORFNames=A9J31_06495 {ECO:0000313|EMBL:OBX28207.1};
OS   Acinetobacter gandensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1443941 {ECO:0000313|EMBL:OBX28207.1, ECO:0000313|Proteomes:UP000185753};
RN   [1] {ECO:0000313|EMBL:OBX28207.1, ECO:0000313|Proteomes:UP000185753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4275 {ECO:0000313|EMBL:OBX28207.1,
RC   ECO:0000313|Proteomes:UP000185753};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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:OBX28207.1}.
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DR   EMBL; LZDS01000026; OBX28207.1; -; Genomic_DNA.
DR   RefSeq; WP_067765399.1; NZ_VZOF01000008.1.
DR   AlphaFoldDB; A0A1A7RBX7; -.
DR   STRING; 1443941.A9J31_06495; -.
DR   OrthoDB; 9777385at2; -.
DR   Proteomes; UP000185753; 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:OBX28207.1};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..449
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008360740"
FT   DOMAIN          227..324
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   449 AA;  48249 MW;  7621420192BFEAF7 CRC64;
     MKKFIQLGAV TLALTTSQMT LADWVKDAAQ AAEVKTIQLR QHIHQYPELG NMEVNTSKLV
     QKELKAYGIQ VKTGFAKTGV IGILKGGKPG PVMALRADMD ALPMQEKTNL SFASKVKAIY
     QGKESPVMHG CGHDAHTAIL LGAAKVLAQH KDQIAGTVVF VFQPAEEGGA DIDNFSEGHL
     IGSRKMISDG AFKDLQPEVI FGLHVIAGIP SGHLHYKTGA ILNSADNLKI TVNGQQVHGS
     MPWAGRDPIV ASAQMINNLQ TVVSRRSDLT QGMGVVSIGQ IQAGTAGNII PEQVSMLGTI
     RSNNEQVRDN ILKTIPQVVE HTAAANDVKA KVEIATYAPV TMNDETLTEV MVPTLKQAAN
     GNVKILNNNA SASEDFAYYG KLMPSLFVFL GATPANQDMS KAAPNHSPFF IVDDATLKTG
     VESHVRFILD YPNVASQVQT AWKNKALKK
//
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