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Beta-lactamase (EC 3.5.2.6)

 Q6ZZU6_BURPE            Unreviewed;       269 AA.
Q6ZZU6; Q63IR9;
05-JUL-2004, integrated into UniProtKB/TrEMBL.
05-JUL-2004, sequence version 1.
22-NOV-2017, entry version 98.
RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140};
EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140};
Name=oxa-59 {ECO:0000313|EMBL:CAG15145.1};
Synonyms=oxa {ECO:0000313|EMBL:ACM89981.1};
ORFNames=ERS012350_04244 {ECO:0000313|EMBL:CFL64596.1};
Burkholderia pseudomallei (Pseudomonas pseudomallei).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Burkholderiaceae; Burkholderia; pseudomallei group.
NCBI_TaxID=28450 {ECO:0000313|EMBL:CAG15145.1};
[1] {ECO:0000313|EMBL:CAG15145.1}
NUCLEOTIDE SEQUENCE.
STRAIN=K96243 {ECO:0000313|EMBL:CAG15145.1};
PubMed=15793160; DOI=10.1128/AAC.49.4.1639-1641.2005;
Keith K.E., Oyston P.C., Crossett B., Fairweather N.F., Titball R.W.,
Walsh T.R., Brown K.A.;
"Functional characterisation of OXA-57, a class D beta-lactamase from
Burkholderia pseudomallei, yields information about beta-lactam
resistance and hydrolysis.";
Antimicrob. Agents Chemother. 49:1639-1641(2005).
[2] {ECO:0000313|EMBL:CAK22313.1}
NUCLEOTIDE SEQUENCE.
STRAIN=316a {ECO:0000313|EMBL:CAK22313.1};
Tansawai U.;
"Characterization of beta-lactamase class D in Burkholderia
pseudomallei.";
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[3] {ECO:0000313|EMBL:CAK22313.1}
NUCLEOTIDE SEQUENCE.
STRAIN=316a {ECO:0000313|EMBL:CAK22313.1};
Niumsup P.R.;
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
[4] {ECO:0000313|EMBL:ACM89981.1}
NUCLEOTIDE SEQUENCE.
STRAIN=76161 {ECO:0000313|EMBL:ACM89981.1};
Sam I.-C., See K.-H., Puthucheary S.;
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
[5] {ECO:0000313|EMBL:ACM89981.1}
NUCLEOTIDE SEQUENCE.
STRAIN=76161 {ECO:0000313|EMBL:ACM89981.1};
PubMed=19297597; DOI=10.1128/JCM.01657-08;
Sam I.C., See K.H., Puthucheary S.D.;
"Variations in ceftazidime and amoxicillin-clavulanate
susceptibilities within a clonal infection of Burkholderia
pseudomallei.";
J. Clin. Microbiol. 47:1556-1558(2009).
[6] {ECO:0000313|EMBL:CFL64596.1, ECO:0000313|Proteomes:UP000047229}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=109/96 {ECO:0000313|EMBL:CFL64596.1,
ECO:0000313|Proteomes:UP000047229};
Pathogen Informatics;
Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000256|RuleBase:RU361140}.
-!- SIMILARITY: Belongs to the class-D beta-lactamase family.
{ECO:0000256|RuleBase:RU361140}.
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EMBL; FJ147202; ACM89981.1; -; Genomic_DNA.
EMBL; AJ632249; CAG15145.1; -; Genomic_DNA.
EMBL; AM263456; CAK22313.1; -; Genomic_DNA.
EMBL; CFWD01000013; CFL64596.1; -; Genomic_DNA.
RefSeq; WP_004524931.1; NZ_NEGN01000063.1.
EnsemblBacteria; CFT98837; CFT98837; ERS012314_04203.
EnsemblBacteria; KIX49370; KIX49370; SY87_04920.
KEGG; ag:CAG15145; -.
KEGG; but:X994_5095; -.
PATRIC; fig|1435366.3.peg.4048; -.
eggNOG; ENOG4108HWY; Bacteria.
eggNOG; COG2602; LUCA.
HOGENOM; HOG000124291; -.
KO; K19209; -.
Proteomes; UP000047229; Unassembled WGS sequence.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
GO; GO:0008658; F:penicillin binding; IEA:InterPro.
GO; GO:0017001; P:antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR002137; Beta-lactam_class-D_AS.
InterPro; IPR001460; PCN-bd_Tpept.
Pfam; PF00905; Transpeptidase; 1.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00337; BETA_LACTAMASE_D; 1.
3: Inferred from homology;
Antibiotic resistance {ECO:0000256|RuleBase:RU361140};
Complete proteome {ECO:0000313|Proteomes:UP000047229};
Hydrolase {ECO:0000256|RuleBase:RU361140,
ECO:0000313|EMBL:CFL64596.1}; Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 23 {ECO:0000256|SAM:SignalP}.
CHAIN 24 269 Beta-lactamase.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5010507352.
DOMAIN 45 250 Transpeptidase.
{ECO:0000259|Pfam:PF00905}.
ACT_SITE 53 53 Acyl-ester intermediate.
{ECO:0000256|PIRSR:PIRSR602137-50}.
MOD_RES 56 56 N6-carboxylysine.
{ECO:0000256|PIRSR:PIRSR602137-50}.
SEQUENCE 269 AA; 29496 MW; 2D69E6E3F72AB49C CRC64;
MKFRHALSSA FVLLGCIAAS AHAKTICTAI ADAGTGKLLV QDGDCGRRAS PASTFKIAIS
LMGYDAGFLR NEHDPVLPYR DSYIAWGGEA WKQPTDPTRW LKYSVVWYSQ QVAHHLGAQR
FAQYAKAFGY GNADVSGDPG QNNGLDRAWI GSSLQISPLE QLEFLGKMLN RKLPVSPTAV
DMTERIVEST TLADGTVVHG KTGVSYPLLA DGTRDWARGS GWFVGWIVRG KQTLVFARLT
QDERKQPVSA GIRTREAFLR DLPRLLAAR


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