ID R7ZVJ8_9BACT Unreviewed; 803 AA.
AC R7ZVJ8;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Penicillin acylase {ECO:0000313|EMBL:EON78171.1};
GN ORFNames=ADIS_1368 {ECO:0000313|EMBL:EON78171.1};
OS Lunatimonas lonarensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae.
OX NCBI_TaxID=1232681 {ECO:0000313|EMBL:EON78171.1, ECO:0000313|Proteomes:UP000013909};
RN [1] {ECO:0000313|EMBL:EON78171.1, ECO:0000313|Proteomes:UP000013909}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK24 {ECO:0000313|EMBL:EON78171.1,
RC ECO:0000313|Proteomes:UP000013909};
RA Singh A.;
RT "A novel strain isolated from Lonar lake, Maharashtra, India.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR001227-2};
CC Note=Binds 1 Ca(2+) ion per dimer. {ECO:0000256|PIRSR:PIRSR001227-2};
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:EON78171.1}.
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DR EMBL; AQHR01000041; EON78171.1; -; Genomic_DNA.
DR RefSeq; WP_010853512.1; NZ_AQHR01000041.1.
DR AlphaFoldDB; R7ZVJ8; -.
DR STRING; 1232681.ADIS_1368; -.
DR MEROPS; S45.003; -.
DR PATRIC; fig|1288963.3.peg.1365; -.
DR OrthoDB; 9759796at2; -.
DR Proteomes; UP000013909; 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:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:InterPro.
DR CDD; cd03747; Ntn_PGA_like; 1.
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:SF4; ACYL-HOMOSERINE LACTONE ACYLASE QUIP; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000013909};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..803
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004451203"
FT ACT_SITE 274
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 179
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 803 AA; 90568 MW; 80717B7DEC3EE5DF CRC64;
MVYRLPPFFS LPSLYLLITL CLASACGSEP RFPDLDAKVT VITDTQGISH IFAESEEDLF
FSQGYLAARN RLFQFELWRR QATGTLSEIL GERELLRDIG VRLFRYRGDK EQELSHYHPR
GVAIVDAFVN GINAYIDEAL RNPEDLPIEF AMLGIQPEKW TWEVVISRHQ GLLQNVQQEL
NYSRIVSLIG PKKTKELFHF HPFDPDLRLS PSIPKELLFK DILAPYAAFR SPLTFLPTDI
EAAYRSQETS AQESGLLDLE QVALESADAA SIGSNNWVIS GELSASGFPI MANDPHRAQA
VPSLRYWVGL HAPGWNLVGG GEPTIPGASI GHNGFGAWGL TIFQTDMEDL RVYDIDPTDP
HRYRYQNRWH RMEKVTDTLR IKDKADTIVH HLYTVHGPVT FIDQSLHKAV AVECAWLRVG
GAPYLASLRM GQAQTWEEFR DACTYNHVPA ENMVWADKAG NIGWQSTGIS PIRLYHSGLV
ASPGDGTADW EGFLPMLDRP SSFNPEVGFI ATANENQVDT NYPHPEALGF TWADSFRGDR
IKEVLATNKK FTVEEMGNLQ NDYLSLPARV LVSELQKIES TDTDVSNVKS LFGTWDYMLN
PESVAAGIYV MWERKIRSNM ATKLIPKEVA PYLTEISMTK TLQWISSNDP GVFGVGEKEE
LLRNSLHQAL NDLTERFGSD WNDWKYGQTG YKHALIRHPL GSVVSDEWRE KLELGPVPRG
GYSFTPGANA YGDNNTTGAS FRIVVDTGDF EQTLGANNPG QSGRHDSPFY RNMFELWWQD
QFFRVPFSKS NVEKKAHSKE TLY
//
