ID   A0A1I4B4K0_9RHOB        Unreviewed;       822 AA.
AC   A0A1I4B4K0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SFK63715.1};
GN   ORFNames=SAMN04488036_101805 {ECO:0000313|EMBL:SFK63715.1};
OS   Shimia haliotis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae.
OX   NCBI_TaxID=1280847 {ECO:0000313|EMBL:SFK63715.1, ECO:0000313|Proteomes:UP000198851};
RN   [1] {ECO:0000313|EMBL:SFK63715.1, ECO:0000313|Proteomes:UP000198851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28453 {ECO:0000313|EMBL:SFK63715.1,
RC   ECO:0000313|Proteomes:UP000198851};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOSZ01000001; SFK63715.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I4B4K0; -.
DR   STRING; 1280847.SAMN04488036_101805; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000198851; 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: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.
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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT   TRANSMEM        7..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        262
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         195
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         334
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         337
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   822 AA;  89993 MW;  326F169812A66FBA CRC64;
     MTLLIQWLLR IASALVILSV CAVIFIYYLA SRSLPDYDKI LQTSAVSASV DIVRDNANVP
     HIFGETDQDV FFALGYAHAQ DRLWQMIMLR RTVQGRLSEA LGTQTLETDT LMRRLDLAGH
     ARASVSAQDA GTLVALKAYA NGVNTRIDEI NLNALGRGAP ELFMFPQSIA PWVPADSIGI
     QKLMALQMTG HLENEVLRAR VSLALSDQKR LDDILPLAPG TGVAALPEYA ALMPDMPRYA
     ASDTAPLSPL SPFPRYGMAG ASNAWAAATS RSASGGTLLA SDPHLGLSAP AIWYLARMEL
     QTGGVIGGTI PGIPAIITGR SDALGWGLTA AHADDQDLFI EELNPDNSQE YRTPNGFAPF
     KTRKSIISIK DAAPVTVTLS WTENGPVLPG SLYNIAAVTP PGHVAALGWT ALSDKDTSLS
     AIMGLMRART IGAAVASTES HIAPVLNLTL ADKENIALKV IGKLPRRDAK HQSKGRLPSL
     GWRTENRWQG TFPYPTNPGF VSPLGGIVGN TNNKVVDRPF PLHMSYVWGD SQRVERWRRL
     MQAREVHTRD SFVEAQLDTV SYTARALLPL VGADLWFTSE AAPDGTRERQ RQRALTLLSE
     WNGEMNEHLP EPLLFAAWMR ALQDRLIRDQ IGPLADSFTH VDPVFIERVF RDIDGASAWC
     DVRQSAPRET CADMARRALD DALISIEERY GSQIEALRWG DAHQAVHNHQ VLGNVPILRF
     FVNIRQSTSG GDNTLQRGLT RGTGPRPFEN VHAAGYRGVY DFADPDSSVF IISTGQSGHF
     LSRFYDDLAQ LWRRGEYIPM SLDIDLARAA AVGVTRILPP DR
//