ID A0A0J6XJA8_9ACTN Unreviewed; 819 AA.
AC A0A0J6XJA8;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-homoserine-lactone acylase {ECO:0000313|EMBL:KMO94337.1};
GN ORFNames=ACS04_29810 {ECO:0000313|EMBL:KMO94337.1};
OS Streptomyces roseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66430 {ECO:0000313|EMBL:KMO94337.1, ECO:0000313|Proteomes:UP000035932};
RN [1] {ECO:0000313|EMBL:KMO94337.1, ECO:0000313|Proteomes:UP000035932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31245 {ECO:0000313|EMBL:KMO94337.1,
RC ECO:0000313|Proteomes:UP000035932};
RA Cruz-Morales P., Martinez-Guerrero C., Morales-Escalante M.A.,
RA Yanez-Guerra L.A., Kopp J.F., Feldmann J., Ramos-Aboites H.E.,
RA Barona-Gomez F.;
RT "Recapitulation of the evolution of biosynthetic gene clusters reveals
RT hidden chemical diversity on bacterial genomes.";
RL Submitted (JUN-2015) 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:KMO94337.1}.
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DR EMBL; LFML01000131; KMO94337.1; -; Genomic_DNA.
DR RefSeq; WP_048479920.1; NZ_LFML01000131.1.
DR AlphaFoldDB; A0A0J6XJA8; -.
DR STRING; 66430.ACS04_29810; -.
DR PATRIC; fig|66430.4.peg.1914; -.
DR OrthoDB; 4759017at2; -.
DR Proteomes; UP000035932; 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; 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 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:UP000035932};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..819
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5039298368"
SQ SEQUENCE 819 AA; 88236 MW; D2C4CC89C53A4263 CRC64;
MARRRFVARL PVAALAVVAV VSTMAAAGPP PARSAAAVAA PDKPTIRYTE YGIPHIIASD
WEGLGTGYGY AAAKDNICTL ADTYLMVNAQ RSRYLGPDGK ASPGEKQNTT SNLNSDLYFQ
RIKDDRVVER LLDQPAPNGP EPEVKEAIRG YVRGYNRYLA ETGADNITDP ACRGASWVRP
ITELDVYRHA HAEIIMGSAD PLLDGQVTAA PAGASAAATP APSPEETAKR IRDAMAVSRR
QSMGSNALAV GSRGVSGGTG MLLANPHFPW QGKNRMWQSQ LTIPGRINVS GASLLGFPAV
NIGHNDDVAW SHTIATVAPF GLFDVQVDPL NPTNYLVDGV WQPMTSQQVA VDVRNADGTL
GKVTRTLWST RYGPIVTSVL GNPLPWVVSA HAVRDVNMGN LRALNTWFHL DQAKDVHEVV
DTLETTEGVP FFNTVASDRK GNALYADIQA TPNISDEHAQ SCLTLTGRLL FNQELRLPNV
PPVSIFDGKR SACDWPTDPN AVAPGLMDPR KQPRLIRSDF VGNANDSAWL ANPEQPLSFP
RVMGDTAAPR SLRTQELILT AQNRINGTDG LPGRGFTPEN MRQLLFADNS RAADLALDAT
VAMCRGVPFG LILVDGTLVN VSEACPVLAA WRSHDFTADS RGSWLFENYW AFLLGGQAIE
KLPWRVPFDP KDPVHTPNSL DSGNSAVRDA FGRAVLALRR AGVALNAPLS DVQKITRNGE
QIPIHGSISE LGVLNVVTPG LVDGKLDITF GSSFVQQVKF TADGPPQTSS VLAYSQSADP
NSPHHVDQTR LFSAGQWVTE RFTEEQIAAS PALETKVLS
//
