ID A0A239EXE1_9ACTN Unreviewed; 1062 AA.
AC A0A239EXE1;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Acyl-homoserine lactone (AHL) acylase PvdQ {ECO:0000313|EMBL:SNS49430.1};
GN ORFNames=SAMN05216276_1010121 {ECO:0000313|EMBL:SNS49430.1};
OS Streptosporangium subroseum.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Streptosporangium.
OX NCBI_TaxID=106412 {ECO:0000313|EMBL:SNS49430.1, ECO:0000313|Proteomes:UP000198282};
RN [1] {ECO:0000313|EMBL:SNS49430.1, ECO:0000313|Proteomes:UP000198282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2132 {ECO:0000313|EMBL:SNS49430.1,
RC ECO:0000313|Proteomes:UP000198282};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOD01000010; SNS49430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239EXE1; -.
DR OrthoDB; 5240333at2; -.
DR Proteomes; UP000198282; 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; 2.60.120.260; Galactose-binding domain-like; 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; IPR000421; FA58C.
DR InterPro; IPR008979; Galactose-bd-like_sf.
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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 1.
DR PANTHER; PTHR34218; PEPTIDASE S45 PENICILLIN AMIDASE; 1.
DR Pfam; PF00754; F5_F8_type_C; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR PROSITE; PS50022; FA58C_3; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000198282};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1062
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012828205"
FT DOMAIN 931..1062
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 318..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1062 AA; 111346 MW; 32382C1661F97C55 CRC64;
MPARLRRKIT AASAVAILTL ASLVVPASAA VFTPADYCLG ECADILPPGE NGNATLVEIL
GNQGFGTMPR HSDDQLGKYA NLISGYTGLT DDQITTFFND GSFGVPAGQV ESTTSPRPDV
KIVRDKATGV PHITGTTRQG TMFGAGYAGA QDRLWVMDLM RHVGRGELTP FAGGAPGNRA
LEQSAWRNSP YTEADLQGQI NRLRDGSPRG AQLYADVQDY VSGINAYIDR CMANRDCPGE
YVLTGHMDAI TNAGGPQDFT MTDLIAISGV IGGLFGGGGG AEMQSALVRV AARAKYGTAA
GDQVWSAFRA QNDPEATLTL HNGQSFPSGN APGATGAVLP DPGTAPVDIT ENETGSATAS
ATASAPAAKG VLEGMLVDNS KPGMSNAVVV SAAKSASGHP VAVFGPQTGY FAPQLLMLQE
ISGPGIQARG AAFSGLNFYV LLGRGADYAW SATSSGQDIT DTYALQLCDP GGGTVTKESK
YYLYHGVCMA METLKKTNAW KPSTADATAA GSYDLVVERT KYGLVSWRGT VGGQPTAFAT
LRSTYQHEAD SAIGFQMFNE TAQMGDAAAF TNSASNIGFA FNWFYVNSSD AAYFMSGNDP
VRSAVSDPNL PMPADAAHEW AGFDPSTNTA TYKAPATHPQ TADQDYLVSW NNKQAKDYGA
ADGNFSFGPV QRADLLDAPV KAALSGSGKL DRAGTVKIMA EAATTDLRGK KVLPDLLRVI
NSATVTDPAL ASAVSKLSAW AASGARRLET SQGSKAYTNA DAIRAFDAWW PKLVNAQFKP
GLGAGLYQSL VNALQINESP SGHQQGDLSS LPTSANEAQT HKGSSFQYGW WGYVSKDVRS
VLGDPVTGPL PSKYCGDGTV AGCRTVLLNS LSAALAEPAA TTYPADDACS AGDQWCADSV
RQSPLGGIKQ SLISWQNRPT YQQVVSFPAH RGDPIANLAS GGTVKASESQ LFYPASAAVD
GDPTTRWGSG WNDNQYLQVD LGSAKTVARA VLRWESAYGS AYSIQTSANG STWTTVCSTT
TGNGGVDNVT FSPVSARYVR MQGAARATSY GYSLYELEAY SR
//