ID A0A1Y1SDQ2_9GAMM Unreviewed; 815 AA.
AC A0A1Y1SDQ2;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Aculeacin-A acylase {ECO:0000313|EMBL:ORE87099.1};
GN ORFNames=ATO7_08667 {ECO:0000313|EMBL:ORE87099.1};
OS Oceanococcus atlanticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Oceanococcus.
OX NCBI_TaxID=1317117 {ECO:0000313|EMBL:ORE87099.1, ECO:0000313|Proteomes:UP000192342};
RN [1] {ECO:0000313|EMBL:ORE87099.1, ECO:0000313|Proteomes:UP000192342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-S10r2 {ECO:0000313|EMBL:ORE87099.1,
RC ECO:0000313|Proteomes:UP000192342};
RA Lai Q., Li G., Shao Z.;
RT "Oceanococcus atlanticus 22II-S10r2 Genome Sequencing.";
RL Submitted (APR-2013) 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:ORE87099.1}.
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DR EMBL; AQQV01000002; ORE87099.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1SDQ2; -.
DR STRING; 1317117.ATO7_08667; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000192342; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000192342};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..815
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5013050437"
SQ SEQUENCE 815 AA; 88193 MW; 43F12D6FFDE5DC40 CRC64;
MRSCCQLTLA LLMALGLLGC NGGRQTHPDP GDAAQNTLST ITRTAGGVPH IESESWFGLG
YGYGYVAAKD AICRIAEFYV TAAGERSRYF GGDNDFPFPA NGFTYNNLNS DFFFKLIRAQ
GTVEQLASEA PPLGPDREIR ALFAGHVAGY NRYLAETGVD GISDPNCRGA AWVRPISVDD
VFRMAYTLAI FAGSAASVDG IGGAAPLLNA SADDVPAILE GLRNAQDWHP GGHLASNAVA
IGRQASVDGT PILLGNPHQT FNDSGIFYQA SFRIPGEAEL SGTTFLGLPF VVMGNNRDVA
WSHTTSSAFR FTPYQMLLAG SHSYVIDGEV EAMQAWPLQV ESRQDDGSLQ RVERTLYTTR
FGPMVTNIAG LPLFVWTPVL GFALADPNAH NMRYLNHFVA LAKVKSVREF EALLDGLQGI
PWANTVAVDR AGEAFYADIT VAANVDDAKA VSCGSVVGLV TFPLLGLPVM DGSRSACAWD
NDPDAVAPGI FGPARLPRLF RDDYVSNSND SYWLSHPDEP LTGFPRILGE EGTERRLRTR
LGLNMIEARL AGTDGFTGRG FSHAIMKDWL FSSRQYLGEM WRDDLLSLCQ QLGMAVGTQG
PIDIADACPV LEGWDLTTNL DSPGALLFRR IAGRLLGQTL PSGTTTQTRL PGTSAFLIPF
RPDEPIDTPR GLNTLLPSVQ AALADAVAEL KAANIPLDAT LRDYQYIERG GQRFALHGGI
DRMGSYSIMN IEWDPQKGYA NPYHGNTYMQ VVSFPPQACP RLSTLTTYSQ SPDPSSPYHT
DQTAMYSDKQ WLEVPFCADA IAAQAIETIH LSSSP
//
