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Database: UniProt
Entry: Q1LBI2_CUPMC
LinkDB: Q1LBI2_CUPMC
Original site: Q1LBI2_CUPMC 
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
//
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