(data stored in SCRATCH zone)
SWISSPROT: B2UI95_RALPJ
ID B2UI95_RALPJ Unreviewed; 809 AA.
AC B2UI95;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 08-MAY-2019, entry version 67.
DE SubName: Full=Peptidase S45 penicillin amidase {ECO:0000313|EMBL:ACD29296.1};
GN OrderedLocusNames=Rpic_4199 {ECO:0000313|EMBL:ACD29296.1};
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29296.1, ECO:0000313|Proteomes:UP000002566};
RN [1] {ECO:0000313|Proteomes:UP000002566}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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-
CC 2};
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DR EMBL; CP001069; ACD29296.1; -; Genomic_DNA.
DR RefSeq; WP_012430258.1; NC_010678.1.
DR EnsemblBacteria; ACD29296; ACD29296; Rpic_4199.
DR GeneID; 6285630; -.
DR KEGG; rpi:Rpic_4199; -.
DR PATRIC; fig|402626.5.peg.449; -.
DR eggNOG; ENOG4105CUJ; Bacteria.
DR eggNOG; COG2366; LUCA.
DR HOGENOM; HOG000093944; -.
DR KO; K01434; -.
DR OMA; YMAFSFA; -.
DR OrthoDB; 186419at2; -.
DR BioCyc; RPIC402626:GH94-4192-MONOMER; -.
DR Proteomes; UP000002566; Chromosome 2.
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; 1.10.439.10; -; 1.
DR Gene3D; 3.60.20.10; -; 1.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR014395; Pen/GL7ACA/AHL_acylase.
DR InterPro; IPR023343; Penicillin_amidase_dom1.
DR InterPro; IPR002692; S45.
DR PANTHER; PTHR34218; PTHR34218; 1.
DR Pfam; PF01804; Penicil_amidase; 1.
DR PIRSF; PIRSF001227; Pen_acylase; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 4: Predicted;
DR PRODOM; B2UI95.
DR SWISS-2DPAGE; B2UI95.
KW Calcium {ECO:0000256|PIRSR:PIRSR001227-2};
KW Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001227-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
FT CHAIN 24 809 {ECO:0000256|SAM:SignalP}.
FT /FTId=PRO_5002783551.
FT ACT_SITE 266 266 Nucleophile. {ECO:0000256|PIRSR:
FT PIRSR001227-1}.
FT METAL 184 184 Calcium. {ECO:0000256|PIRSR:PIRSR001227-
FT 2}.
FT METAL 338 338 Calcium. {ECO:0000256|PIRSR:PIRSR001227-
FT 2}.
FT METAL 341 341 Calcium. {ECO:0000256|PIRSR:PIRSR001227-
FT 2}.
SQ SEQUENCE 809 AA; 89787 MW; 11CA0D796C3853DE CRC64;
MPIRSLSILL SAVALGFSAQ AVAKDAHTAA AQTIAVPGLS KPADILIDRW GVPHIYARSE
DDGFFAQGFN AARDRLFQID LWRRRGLGQL SEVFGPAYVE QDRATRLFLY RGDMQVEWNH
YSPDAQRIAT RFVAGINAYV DWLAKHPEQM PFEFRKLNYA PAHWAPEDVV RIRSHGLTRN
LQSEVARANV ACKANLSDDT VRFRLQPAWQ TQLPEGLDPC LPKDLLRVFT LATQGARLTP
ESLKGVDVDS TRVAAAANLE ETMEGSNNWV IAPGKSTTGR AVMANDPHRA YSAPSLRYIA
HVSTPTLDII GAGEPSLPAV SIGHNGHVAF GLTIFNIDQE DLYVYELNPA NNGEYRYNGG
WEPFIVLHET VKVRGGESRP VDLTFTRHGP VIYIDAEKHR AYAVRSAWLS PGMSPYFGSV
GYMRARTFAQ FRQSMMNWGA PTENQVYADT KGNIGWVPGG LAPIRPNWDG LLPVPGDGRY
EWAGFWRGDQ LPSSYNPKSG YFTSSNEMNL PADYPYRERK LGFEWTNGSR HVRIDEVLSK
LDKVSIEDSM RLQNDMVSIP ARRLTALLAP LSSDDADTQA ALNLFKGWNA TMLADSPQAA
LHEVWFTHHL GRAFKNAVLS KASAEAMAAP DTDVMLDTLE HPQGSDRKFG EDPQQAAAKR
DAVLLDSLKN AWTDMVKRQG PNPQAWNWGQ LHHNLNAHPF TAIVDEATRA KLNVGPTPEG
GSPYTPNQST YRASDFLQTN GPSFRTVVDV GKWDNSRAVN LPGQSGNPDS PHYRDLAPLW
LKGKYFPLLY SRKAVEAATE SRVHLVPGK
//
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