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Beta-lactamase (EC 3.5.2.6)

 S0F1K6_ECOLX            Unreviewed;       291 AA.
S0F1K6;
18-SEP-2013, integrated into UniProtKB/TrEMBL.
18-SEP-2013, sequence version 1.
27-SEP-2017, entry version 23.
RecName: Full=Beta-lactamase {ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00129357};
EC=3.5.2.6 {ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00129357};
Name=blaCTX-M-19 {ECO:0000313|EMBL:CDF31571.1};
Escherichia coli.
Plasmid pEC1737 {ECO:0000313|EMBL:CDF31571.1}.
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=562 {ECO:0000313|EMBL:CDF31571.1};
[1] {ECO:0000313|EMBL:CDF31571.1}
NUCLEOTIDE SEQUENCE.
STRAIN=EC1737 {ECO:0000313|EMBL:CDF31571.1};
PLASMID=pEC1737 {ECO:0000313|EMBL:CDF31571.1};
Garcia-Fulgueiras V., Bado I., Cordeiro N.F., Algorta G., Vignoli R.;
"First Report of the Ceftazidimase CTX-M-19 in South America.";
Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
[2] {ECO:0000313|EMBL:CDF31571.1}
NUCLEOTIDE SEQUENCE.
STRAIN=EC1737 {ECO:0000313|EMBL:CDF31571.1};
PLASMID=pEC1737 {ECO:0000313|EMBL:CDF31571.1};
Garcia-Fulgueiras V.;
"Resistencia transferible a oxiiminocefalosporinas y quinolonas en
ninos que se asisten en el Centro Hospitalario Pereira Rossell.
Caracteristicas Clinicas y Microbiologicas.";
Thesis (2014), Department of Bacteriology and Virology, Universidad de
la Republica, Montevideo, Uruguay.
-!- CATALYTIC ACTIVITY: A beta-lactam + H(2)O = a substituted beta-
amino acid. {ECO:0000256|RuleBase:RU361140,
ECO:0000256|SAAS:SAAS00129358}.
-!- SIMILARITY: Belongs to the class-A beta-lactamase family.
{ECO:0000256|RuleBase:RU361140, ECO:0000256|SAAS:SAAS00559532}.
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EMBL; HG000669; CDF31571.1; -; Genomic_DNA.
ProteinModelPortal; S0F1K6; -.
SMR; S0F1K6; -.
GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
InterPro; IPR012338; Beta-lactam/transpept-like.
InterPro; IPR000871; Beta-lactam_class-A.
InterPro; IPR023650; Beta-lactam_class-A_AS.
PRINTS; PR00118; BLACTAMASEA.
SUPFAM; SSF56601; SSF56601; 1.
PROSITE; PS00146; BETA_LACTAMASE_A; 1.
3: Inferred from homology;
Antibiotic resistance {ECO:0000256|RuleBase:RU361140,
ECO:0000256|SAAS:SAAS00063120};
Hydrolase {ECO:0000256|RuleBase:RU361140,
ECO:0000256|SAAS:SAAS00483625}; Plasmid {ECO:0000313|EMBL:CDF31571.1};
Signal {ECO:0000256|SAM:SignalP}.
SIGNAL 1 28 {ECO:0000256|SAM:SignalP}.
CHAIN 29 291 Beta-lactamase.
{ECO:0000256|SAM:SignalP}.
/FTId=PRO_5004486306.
SEQUENCE 291 AA; 30969 MW; C8DDCD742EAE469D CRC64;
MVTKRVQRMM FAAAACIPLL LGSAPLYAQT SAVQQKLAAL EKSSGGRLGV ALIDTADNTQ
VLYRGDERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTES TLNTAIPGDP
RDTTTPRAMA QTLRQLTLGH ALGETQRAQL VTWLKGNTTG AASIRAGLPT SWTVGDKTGS
GDYGTTNDIA VIWPQGRAPL VLVTYFTQPQ QNAESRRDVL ASAARIIAEG L


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