ID   A0A1G7IKW5_9BACT        Unreviewed;       738 AA.
AC   A0A1G7IKW5;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   SubName: Full=Acyl-homoserine-lactone acylase {ECO:0000313|EMBL:SDF13184.1};
GN   ORFNames=SAMN05444167_1484 {ECO:0000313|EMBL:SDF13184.1};
OS   Terriglobus roseus.
OC   Bacteria; Acidobacteriota; Terriglobia; Terriglobales; Acidobacteriaceae;
OC   Terriglobus.
OX   NCBI_TaxID=392734 {ECO:0000313|EMBL:SDF13184.1, ECO:0000313|Proteomes:UP000182427};
RN   [1] {ECO:0000313|EMBL:SDF13184.1, ECO:0000313|Proteomes:UP000182427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS232 {ECO:0000313|EMBL:SDF13184.1,
RC   ECO:0000313|Proteomes:UP000182427};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S45 family.
CC       {ECO:0000256|ARBA:ARBA00006586}.
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DR   EMBL; LT629690; SDF13184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G7IKW5; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000182427; Chromosome i.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR   Gene3D; 1.10.1400.10; -; 1.
DR   Gene3D; 2.30.120.10; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   Gene3D; 1.10.439.10; Penicillin Amidohydrolase, domain 1; 1.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR   InterPro; IPR043147; Penicillin_amidase_A-knob.
DR   InterPro; IPR023343; Penicillin_amidase_dom1.
DR   InterPro; IPR043146; Penicillin_amidase_N_B-knob.
DR   InterPro; IPR002692; S45.
DR   PANTHER; PTHR34218:SF3; ACYL-HOMOSERINE LACTONE ACYLASE PVDQ; 1.
DR   PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR   Pfam; PF01804; Penicil_amidase; 1.
DR   PIRSF; PIRSF001227; Pen_acylase; 2.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000182427};
KW   Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..738
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009241438"
FT   ACT_SITE        202
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
SQ   SEQUENCE   738 AA;  82689 MW;  6977D49973259FF6 CRC64;
     MPLRRRILSA ALIAAACLPA LAQPKYKPQK GSEILWDKWG VPHIFAKSTK DMFYLYGYAQ
     TEAHGELLMH VMAGSRGRSS EIYGPGDGDK NLKTDRWVLL NEVPKRSQLW LSQQTPEFRS
     YLEAFAAGIN AYAAKHPDKL SAEAKQVLPI TALDIVQHTH HFVNFEFVAS NRLMNARDTE
     TAELRMPESP YSPTNMDMQD GSNGWAIAPS HTASGNAMLL MNPHLAMAGE QSYFEAQLVA
     PGINLFGASQ VGLPVMRFCF SDYVAITNTV NTNNGALQFA IKEQDGGYLY DGKVLKYETA
     QYPFRIKQKD GSLTTEIVQV QKTVHGPIVR RDNGIPIALY AAGLDKPFFL EQYWKMDTAH
     NLAEYQTQLK RLEVPMYNIL YADRDGHIEY LFNANVPRRT GDWAMWTKPV DGSISTTKPH
     GILSYDELPK QVDPASGYVQ NSNQPPWDAA WPTMIDRAKY PAYVSSFFPL FRSDRALRML
     SEDKKFTFDM LLQKKFSTRM EMADRMMDDL QSAVAQYGSP KAKKAAEILK NWDHTTEANS
     RGAFLFYVWA QKFIGPTVGM QTPKSMQNFA VPYDYNQPLT TPRGIKDPKL AAQMLDAAYD
     ETAKTYGAPD RPWGEVMKFE INGQSDGNTS APRGEAINGV SLPGNGGPGN LGIFRVITWG
     PMLNGTKTPV HGDGFTVALE FSKTGVKQAK TFVYYGESSQ LGSPFHTDEL PLAEKKQWRD
     VWRTRKEILA NLSSKEVF
//