ID   A0A0P8YY50_9RHOB        Unreviewed;       820 AA.
AC   A0A0P8YY50;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Penicillin acylase {ECO:0000313|EMBL:KPU83846.1};
GN   ORFNames=JI58_07315 {ECO:0000313|EMBL:KPU83846.1};
OS   Marinosulfonomonas sp. PRT-SC04.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Marinosulfonomonas.
OX   NCBI_TaxID=1527300 {ECO:0000313|EMBL:KPU83846.1, ECO:0000313|Proteomes:UP000054415};
RN   [1] {ECO:0000313|EMBL:KPU83846.1, ECO:0000313|Proteomes:UP000054415}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PRT-SC04 {ECO:0000313|EMBL:KPU83846.1};
RA   Leon Zayas R.I., Novotny M., Podell S., Shepard C.M., Berkenpas E.,
RA   Nikolenko S., Pevzner P., Lasken R.S., Bartlett D.H.;
RT   "Microbial Metabolic Properties Below 8,000 Meters Depth Within the Puerto
RT   Rico Trench Inferred From Single Cell Genomes.";
RL   Submitted (AUG-2014) 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:KPU83846.1}.
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DR   EMBL; JPUR01000224; KPU83846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P8YY50; -.
DR   PATRIC; fig|1527300.3.peg.1551; -.
DR   Proteomes; UP000054415; 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   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   Reference proteome {ECO:0000313|Proteomes:UP000054415};
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        261
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         333
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT   BINDING         336
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   820 AA;  90612 MW;  AACF5F89D3E30FB8 CRC64;
     MAFAFRWLTR IFIGLFALAL LAGFLVYYLA SRSLVDYDAT HQVTGLTEAV EIVRDNANVP
     HIFGATDTDV FYALGFAHAQ DRLWQMTMLR RTVQGRLSEQ FGMQTLATDK MMRRFDLYNL
     AVQSVQVQDA ATKLVLEAYA KGVNAWLTEI NKGALGRGAP EFFLFSSQIA PWQPADSIAI
     IKLMALKMSS HLDQEVLRAQ TSLLLPNQRL RDILPDAPGT AIAALPNYAS LFPNLPRYAA
     NTPARRDPLS PFKSRAFAGA SNAWAAAPKR SAAGGTLLAN DPHMSFSAPS IWYLARLELK
     QGGIIGGTIP GVPAILVGRS DFLGWGLTAA YVDDLDVYIE RLNPDNADEY QTASGFKPFV
     SRDSIIRIKD ATPVTIKLQW SDNGPVLPGS HFDLASITPA GHVTTVAWTA LSPVDTTMSA
     VLGMMQSRSI AQALRNTKRY LVPAMNLTLA DGDQIAMKTI GAIPKRDINH QTQGRIPSQG
     WLAENRWQGR ADYADNPEFL NPVGGIIGNT NNKTVDRPFP RHVSYVWGDT QRILRWKRLM
     QSREVHTRES FIEAQLDTVS YTARALLPLI AADLWFTGEA AAEGSKAHRR QQALDMLANW
     NGEMNEHLPE PLIYAAWLRA LQERLIKDEL GPLAAKYSHV EPLFIERVYR NTGGAKIWCD
     VLQSAVIESC TDIARLALDD ALLWITENHG TALEALRWGD AHQATHDHQV LGKIPVLKWF
     VNIRQSTSGG DNTLMRGLSS GQDPTPFQNV HGASFRGVYD FADPDSSVFV IPTGQSGHPL
     SRFYDNLGEL WRRGEYIPMS LDPELARAAA AGIAHLQPVQ
//