ID A0A1A5X970_9BURK Unreviewed; 775 AA.
AC A0A1A5X970;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Acyl-homoserine-lactone acylase {ECO:0008006|Google:ProtNLM};
GN ORFNames=A6456_33850 {ECO:0000313|EMBL:OBR50056.1};
OS Paraburkholderia tropica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=92647 {ECO:0000313|EMBL:OBR50056.1, ECO:0000313|Proteomes:UP000093802};
RN [1] {ECO:0000313|Proteomes:UP000093802}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P-31 {ECO:0000313|Proteomes:UP000093802};
RA Kaur C., Selvakumar G., Ganeshamurthy A.N.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S45 family.
CC {ECO:0000256|ARBA:ARBA00006586}.
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:OBR50056.1}.
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DR EMBL; LXGI01000081; OBR50056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1A5X970; -.
DR Proteomes; UP000093802; Unassembled WGS sequence.
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; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000093802};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..775
FT /note="Acyl-homoserine-lactone acylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5008339356"
FT ACT_SITE 214
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
SQ SEQUENCE 775 AA; 84229 MW; 8898DA392186A7C3 CRC64;
MRFVAIAGVV LSLVASTVYA KADSDATVEI RRTSFGIPHI KANSERGLGF GIGFAYAQDN
VCLLAQDVVT ARGDRSRYWG DDAKNEDGTS NLESDFFFKW YNTDAAVNAF WGAQPQAIQD
LLTGYADGYN HYLAVHNTTD LPASCRAQWV APITREDLVR VTRKLLIRAG FAQFERAIVA
AIPPSSPVGS QSQIDHDGDG PLEALDRFPT RYGSNGVAVG HALSGGGGLL LGNPHFPWSG
ALRFYQMQLT IPGRLNVMGA ALPGLPVINI GFNHDVAWTH TVDTSAHFTL YRLKIDPANP
THYLKDGQSL PLRKTTVTVN VKSKDGAVET KSHDFYESEN GPLLSWPGQF PWSATQAFSI
RDANQNNTRV LAQWLEIDQA RNVEQLRHSL IQTVGIPWVD TVAADANGKV MFANISAIPG
LSAEHLKACE LPLDAAHSRI VLLDGSRSTC DWTNDSELVG QANLPGKTLP SLVRDDFVQS
SNDSAWLANP AEPLVGFPAT VSREDVPLGG RSRFALDWLS RRIESGRGVG AQDLGRMVTD
NRVFLAFVAL DDMLRLCDGD AQRSSHADKE QLAQACRALR SWDRTANTNA GLGYVYFDAA
MSRVRNTPDA WAVPFDPAHP VATPYGLRVD DPKIAAEVTN ALVSTAAAIK RSGLPENATW
GNIQIATRNG QAIPIPGGDG PLGVYNAIES RPAADGRREV AYGSSYMQVV ALTPNGPKAQ
TLLTFSESTD PTSAHFADQT ELFSRNEWIN IPFTEADIRA DAHYRLTVLR DAARQ
//
