ID A0A238YJP5_9RHOB Unreviewed; 820 AA.
AC A0A238YJP5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Penicillin amidase {ECO:0000313|EMBL:SNR71182.1};
GN ORFNames=SAMN06265370_11776 {ECO:0000313|EMBL:SNR71182.1};
OS Puniceibacterium sediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Puniceibacterium.
OX NCBI_TaxID=1608407 {ECO:0000313|EMBL:SNR71182.1, ECO:0000313|Proteomes:UP000198417};
RN [1] {ECO:0000313|EMBL:SNR71182.1, ECO:0000313|Proteomes:UP000198417}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29052 {ECO:0000313|EMBL:SNR71182.1,
RC ECO:0000313|Proteomes:UP000198417};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FZNN01000017; SNR71182.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238YJP5; -.
DR OrthoDB; 9760084at2; -.
DR Proteomes; UP000198417; 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 Reference proteome {ECO:0000313|Proteomes:UP000198417};
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 REGION 729..748
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 729..747
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 820 AA; 90256 MW; 425F9498A2174E6E CRC64;
MGFLFRWLLR LASAAVVLTV LAVLVVYYLG SRSLPDYNKT LVVSGLTGDV EIVRDNSNVP
HIMAQSDEDA FYGLGYAHAQ DRLWQMTLLR RTVQGRLSEI FGARTVETDK LLRRLDLYPL
AVLSVDAQDA RTRAALESYS AGVNARIAEI NRDSLGRGAP EFFLFNAPLS PWRPADSIAI
VKLMALQLSG QMRDEVLRAR TSLLLPDADR VADILPDMPG EGVAALPEYA SLFPDLPQFA
QGQNIGNDML MPVAPRGLAG ASNAWAAAPS RSASGGTLLA NDPHLSFTAP SIWYLARLQL
SSGGVIGGTI PGVPAIMLGR SEKLGWGITS SYLDDQDLYI EELNPENPEQ YRTPDGWSRF
RTRKSIIDIK DSAPITVTLR WTENGPVLPG TQFDLNTVTP PGHVATLAWT ALSARDTSMS
AAIGMMHAGS VTEALKVSEG YVAPSQNLTL IDRDTIALKT VGAMPRRDAN HQSLGRLPSP
GWRSENRWQG ILPYSTNPEF VAPAGGIVGN TNNKIIDRPF PMHMSFDWGD SQRVVRWQGL
MQGRQVHTRD SFIEAQLDTV SVTARTLLPL IGADLWYTGE AAPDGTPERQ RQRALQLLAD
WNGEMNEHLP EPLIYAAWLR ALQQRLIRDE LGPLAEEFDH VEPLFIERVY RDVDGASVWC
DILRSAPVET CTQIAQLALD DALVWIGEKF GTNLESLRWG EAHQATHDHT VLGKMPVLRY
FVNIRQSTSG GDNTLQRGQT SGQDPDPFQN VHGVGYRGVY DFADPDSSVF VTATGQSGHF
LSRHYDDLGQ LWRRGEYIPM SLDLDLAQAA AVGITHLVPE
//
