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Database: UniProt
Entry: A0A208XPL4_9BURK
LinkDB: A0A208XPL4_9BURK
Original site: A0A208XPL4_9BURK 
ID   A0A208XPL4_9BURK        Unreviewed;       813 AA.
AC   A0A208XPL4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Penicillin acylase family protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=CDO44_15965 {ECO:0000313|EMBL:OVZ57881.1};
OS   Pigmentiphaga sp. NML080357.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Pigmentiphaga.
OX   NCBI_TaxID=2008675 {ECO:0000313|EMBL:OVZ57881.1, ECO:0000313|Proteomes:UP000196551};
RN   [1] {ECO:0000313|EMBL:OVZ57881.1, ECO:0000313|Proteomes:UP000196551}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NML080357 {ECO:0000313|EMBL:OVZ57881.1,
RC   ECO:0000313|Proteomes:UP000196551};
RA   Bernier A.-M., Bernard K.;
RT   "Pigmentiphaga species Genome sequencing and assembly.";
RL   Submitted (MAY-2017) 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:OVZ57881.1}.
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DR   EMBL; NINW01000037; OVZ57881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A208XPL4; -.
DR   OrthoDB; 9760084at2; -.
DR   Proteomes; UP000196551; 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        12..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          224..261
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..240
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        278
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT   BINDING         357
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ   SEQUENCE   813 AA;  87319 MW;  858AD5ADAF81D213 CRC64;
     MTRRVASRAV RLAALATAGL VVLMVMSAAG AWLYLRASLP QLDGQVRAGT MQSATIARDA
     QGSVTIRAQN RADAAYATGF AHAQDRFFQM DLVRRSAAGE LAALVGEAAV PMDRRVRLHR
     FRTRAERAYA ALPPAHRTLL ERYADGVNAG LASLDARPFE YVLLGAPPQP WQPVDTLLAI
     YAMYLDLQGG ELVRTRSREA LRSLLPEPVL AALIPVGSRW DAPLDRPPSS APPEVPPAPA
     LLDARPDWID RPRPPRTRGA TPAELMVDAG TPASALGSNG WAVDARRGAD GRALVANDMH
     LGLRLPNVWY RLTLEFPSAA GQRRISGVSL PGAPIVVAGS NGDIAWGFTN SYGHFMDLVR
     LDPDPADPTR YRGPADAWEP ASETMERIEV KDGPPVMLPV RETRWGPVLQ TGAHAYAVRW
     IAHLPEAANV VLAEMENARD LGQALRVAQA AGIPTQNLVA ADRGGGIGWT LAGPLPAATL
     DPLGFPAEPD RAGAPLARLA PADYPAIIDP AYGRLWTANS TQLADGDAQR KIGDGGADVG
     ARATQIRDAL FAAERFNERD LLAIQLDDRA PWIAFLREQA LAVLDDAAVA DHPQRAAARR
     ILQSWNGRAD ADSAGYALLR AYYDALYDAW FGALDDRLAA IEPGLSVRRA SSRLLAVMED
     LVRAQAWKPA YAADWRAFML ERIDTSIAAL TAGGRPLEKI RWGDRNRLAI AHPLARVLPA
     PVGRWLSAPR RPMPGDIHMP RVQGAAFGAS ERFVVSPGHE EHGVLEMPGG ASGHPLSPFF
     LAGHSAWVAG EASPFLPGPD AHRLTLAPAE AGH
//
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