ID Q1LBI2_CUPMC Unreviewed; 812 AA.
AC Q1LBI2;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 95.
DE SubName: Full=Penicillin amidase (Peptidase S45) {ECO:0000313|EMBL:ABF12494.1};
DE EC=3.5.1.11 {ECO:0000313|EMBL:ABF12494.1};
GN OrderedLocusNames=Rmet_5635 {ECO:0000313|EMBL:ABF12494.1};
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OG Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429}.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264 {ECO:0000313|EMBL:ABF12494.1, ECO:0000313|Proteomes:UP000002429};
RN [1] {ECO:0000313|Proteomes:UP000002429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34
RC {ECO:0000313|Proteomes:UP000002429};
RC PLASMID=Plasmid megaplasmid CH34 {ECO:0000313|Proteomes:UP000002429};
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000353; ABF12494.1; -; Genomic_DNA.
DR RefSeq; WP_011520038.1; NC_007974.2.
DR AlphaFoldDB; Q1LBI2; -.
DR MEROPS; S45.003; -.
DR KEGG; rme:Rmet_5635; -.
DR eggNOG; COG2366; Bacteria.
DR HOGENOM; CLU_011790_0_1_4; -.
DR OMA; MDELPWA; -.
DR Proteomes; UP000002429; Plasmid megaplasmid CH34.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008953; F:penicillin amidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABF12494.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Plasmid {ECO:0000313|EMBL:ABF12494.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002429};
KW Signal {ECO:0000256|SAM:SignalP}; Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..812
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004193038"
FT ACT_SITE 278
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-1"
FT BINDING 184
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000256|PIRSR:PIRSR001227-2"
SQ SEQUENCE 812 AA; 90379 MW; 9E8BA8E3F466ABD5 CRC64;
MFRPTRSLRR TAVAAAWLAA ASTAPALAAG PDKFAVPGLE KPATVLIDRW GVPHIYANTL
YDAFFVQGFV AARDRLFQID LWRKRGLGEM AKDFGPAYVE GDRMARAVLF RGDMYREWLA
YGSDAKRVAE AFVAGVNAYI AQTEAHPELL PPEFKLINYK PSRWRAEDIV RIRHHGLTLN
LTGEIDRAQI FCYAKPNAVR ADWVRRELDP QIEPKVPDGL DPCTVPAAEL RKAYELATAA
PRFPKDVWQS GTRAENIPVD QLYATVDASS DTARSLGSNN WVIAGSRTAT GRPILANDPH
RAHGAPSLRY ISHLNAPGLS VIGAGEPFLP GISIGHNGTI AFGLTRFYMD QEDLYAYETD
PAQPHEYKYK GRWEPMETVT EQISVRGEAT PRKVTIDFTR HGPVLYADSK NNRAWALRAA
WLDLGMAPYF GSMDYMRAQN WDQFRAAMNR WGAPGENQVY ADRFGNIGWL PGGLTVNRPN
WDGLMPVPGD GRYEWAGYRN MDELPWAFNP APGFVVTANE NTIPPNHPAA KLGVGYEWAE
SSRARRLRAL VSANPRSSVE DSMAWQNDTV SLPAQRMVTL LKPLASSDAQ IQRGLDLLRG
WDGNERADSA PAALFEVWFS KHLRTAVVRA ALAPEAARLI GAGDPSRVIA VLERPDSWMS
VEKRNDVMLA SLKSAMVEVE KRLGPDPKTW QWGKLHTAVF EHPLHAILDA QQRQQFDVNA
GPIGGSSFTP MNTSYRNNDF QLTAGASFRM VVDVGNWDAS RVVNTPGQSG NPANPHYRDL
APLWAKGEYF PLLYSRKAVE KESKERLELV PQ
//