(data stored in SCRATCH zone)

SWISSPROT: B2UHL6_RALPJ

ID   B2UHL6_RALPJ            Unreviewed;       271 AA.
AC   B2UHL6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140};
DE            EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140};
GN   OrderedLocusNames=Rpic_3962 {ECO:0000313|EMBL:ACD29067.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29067.1, 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=a beta-lactam + H2O = a substituted beta-amino acid;
CC         Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627,
CC         ChEBI:CHEBI:140347; EC=3.5.2.6;
CC         Evidence={ECO:0000256|RuleBase:RU361140};
CC   -!- SIMILARITY: Belongs to the class-D beta-lactamase family.
CC       {ECO:0000256|RuleBase:RU361140}.
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DR   EMBL; CP001069; ACD29067.1; -; Genomic_DNA.
DR   RefSeq; WP_012430091.1; NC_010678.1.
DR   STRING; 402626.Rpic_3962; -.
DR   EnsemblBacteria; ACD29067; ACD29067; Rpic_3962.
DR   GeneID; 6285211; -.
DR   KEGG; rpi:Rpic_3962; -.
DR   PATRIC; fig|402626.5.peg.202; -.
DR   eggNOG; ENOG4108HWY; Bacteria.
DR   eggNOG; COG2602; LUCA.
DR   HOGENOM; HOG000296772; -.
DR   KO; K21277; -.
DR   OMA; WNRDHTL; -.
DR   OrthoDB; 1688418at2; -.
DR   BioCyc; RPIC402626:GH94-3963-MONOMER; -.
DR   Proteomes; UP000002566; Chromosome 2.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008658; F:penicillin binding; IEA:InterPro.
DR   GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR002137; Beta-lactam_class-D_AS.
DR   InterPro; IPR001460; PCN-bd_Tpept.
DR   Pfam; PF00905; Transpeptidase; 1.
DR   SUPFAM; SSF56601; SSF56601; 1.
DR   PROSITE; PS00337; BETA_LACTAMASE_D; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2UHL6.
DR   SWISS-2DPAGE; B2UHL6.
KW   Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Hydrolase {ECO:0000256|RuleBase:RU361140,
KW   ECO:0000313|EMBL:ACD29067.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     27       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        28    271       Beta-lactamase. {ECO:0000256|SAM:
FT                                SignalP}.
FT                                /FTId=PRO_5002783522.
FT   DOMAIN       66    263       Transpeptidase. {ECO:0000259|Pfam:
FT                                PF00905}.
FT   ACT_SITE     74     74       Acyl-ester intermediate.
FT                                {ECO:0000256|PIRSR:PIRSR602137-50}.
FT   MOD_RES      77     77       N6-carboxylysine. {ECO:0000256|PIRSR:
FT                                PIRSR602137-50}.
SQ   SEQUENCE   271 AA;  30437 MW;  78AA30656943764B CRC64;
     MFSRWSKTFA SALTACAVAM STTTAHAELV VRNDLKRAFD DAGVSGTFVL MDIGADRTYV
     VDPARAARRI HPASTFKIPN SLIAFDTGAV RDDQEVLPYG GKPQPYQQWE HDMALPEAIR
     LSAVPIYQEV ARRVGLERMQ AYVDAFEYGN RQLGSVIDQF WLRGPLEISA FEEARFTSRM
     ALKQLPVKPR TWDMVQRMLL IEQQGDAALY AKTGVATEYQ PEIGWWVGWV ERAGHVYAFA
     LNIDMPREGD MAKRVPLGKQ LMQALAVWPA P
//

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