ID   A0A1B8TRW0_9FLAO        Unreviewed;       794 AA.
AC   A0A1B8TRW0;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:OBY62342.1};
GN   ORFNames=LPB301_14615 {ECO:0000313|EMBL:OBY62342.1};
OS   Polaribacter reichenbachii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae.
OX   NCBI_TaxID=996801 {ECO:0000313|EMBL:OBY62342.1, ECO:0000313|Proteomes:UP000092612};
RN   [1] {ECO:0000313|Proteomes:UP000092612}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 23969 {ECO:0000313|Proteomes:UP000092612};
RA   Shin S.-K., Yi H.;
RT   "Paenibacillus sp. LPB0068, isolated from Crassostrea gigas.";
RL   Submitted (FEB-2016) 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:OBY62342.1}.
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DR   EMBL; LSFL01000036; OBY62342.1; -; Genomic_DNA.
DR   RefSeq; WP_068363750.1; NZ_VRMM01000042.1.
DR   AlphaFoldDB; A0A1B8TRW0; -.
DR   STRING; 996801.BW723_01075; -.
DR   KEGG; prn:BW723_01075; -.
DR   OrthoDB; 9759796at2; -.
DR   Proteomes; UP000092612; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:SF5; PENICILLIN G ACYLASE; 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   Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092612};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        247
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         319
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   794 AA;  90028 MW;  273D0BBFA3459A63 CRC64;
     MKFLKKGLKI VVFLVILIVV LIFVYSKVNE PKYSGELEIK NLSDDVTVYF DEIGVPHINA
     QNQKDAYLAL GYIHAQDRLW QMELIRRIAP GRLSEIFGKD LVSTDVFFSG LGIEEAADKT
     IAGLDKSSDS YMLTQAYLDG INQYLEEGST PLEFRLLGIE KEKYTIKDIY NVFGYMSFSF
     AVAHKTDPLL TEIKEKLGKP YLDEVLGAYS KNLLINKMDS VSKINSNFSK SVSAIMDQMP
     VPPLIGSNSW VIGADKTKNG KVIFANDPHI GYSQPSVWYQ NHIKTPDFEM YGFNIALMPF
     PLLGHNKNYA YGLTMLANDD LNFYIEENNP KNDESYKIEN GYQFYETRTK TINIKGGADT
     TFTVKVSKHG PIMNGIISHL EDERPVAMNW IYTQLKNEML DVSYGISHSN SINDFKKSVA
     KIHAPGLNVM YGDADDNIAW FASAKLYQLR DSLFSKMYLN GASGKDEIIE YLDFSENPKS
     INPKSNYVYS ANHQPDSVRG KLYPGYYQPE NRSKRIVNLL EAKNDFTKQD VAKMLYDVTS
     SVDHNIARDL LKFVSKGELG ASEKQAFSIL ENWEGVYLKT SIAPTIYNRF LFEFLQNTYK
     DELGSGFDLF INSQLQDQVL VNQIDRENSV WWDDISTKNK VETKEEIITK SYKSAIAFLQ
     NQLGANVESW TWDRVISVEH EHAIGKAGGI LRKIFNVGPF KTIGGNEVIN NQIFKLDSTG
     IYKITSGPSS RRVVDFSDVE NSLGIIPTGQ SGNIFSDYYK NQAEKYVDGK FEKMKLNEAE
     IKKSEHVLIL KPKE
//