ID Q5R218_SALEN Unreviewed; 291 AA.
AC Q5R218;
DT 04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT 04-JAN-2005, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Beta-lactamase {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
DE EC=3.5.2.6 {ECO:0000256|ARBA:ARBA00012865, ECO:0000256|RuleBase:RU361140};
GN Name=bla {ECO:0000313|EMBL:BAD72947.1};
GN Synonyms=blaCTX-M-14 {ECO:0000313|EMBL:AQT23959.1};
OS Salmonella enteritidis.
OG Plasmid pS12 {ECO:0000313|EMBL:BAD72947.1}, and
OG Plasmid unnamed {ECO:0000313|EMBL:AQT23959.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=149539 {ECO:0000313|EMBL:BAD72947.1};
RN [1] {ECO:0000313|EMBL:BAD72947.1}
RP NUCLEOTIDE SEQUENCE.
RC PLASMID=pS12 {ECO:0000313|EMBL:BAD72947.1};
RX PubMed=15917576; DOI=10.1128/AAC.49.6.2568-2570.2005;
RA Izumiya H., Mori K., Higashide M., Tamura K., Takai N., Hirose K.,
RA Terajima J., Watanabe H.;
RT "Identification of CTX-M-14 {beta}-lactamase in a Salmonella enterica
RT serovar enteritidis isolate from Japan.";
RL Antimicrob. Agents Chemother. 49:2568-2570(2005).
RN [2] {ECO:0000313|EMBL:AQT23959.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SE380 {ECO:0000313|EMBL:AQT23959.1};
RC PLASMID=unnamed {ECO:0000313|EMBL:AQT23959.1};
RA Wong M.H., Chen S.;
RT "Fusion of virulence plasmid pSEN and IncHI2 resistance plasmid in
RT Salmonella enteritidis.";
RL Submitted (DEC-2016) 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|ARBA:ARBA00001526,
CC ECO:0000256|RuleBase:RU361140};
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000256|ARBA:ARBA00009009, ECO:0000256|RuleBase:RU361140}.
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DR EMBL; KY401053; AQT23959.1; -; Genomic_DNA.
DR EMBL; AB180674; BAD72947.1; -; Genomic_DNA.
DR RefSeq; WP_001617865.1; NZ_QSLT01000034.1.
DR AlphaFoldDB; Q5R218; -.
DR SMR; Q5R218; -.
DR GeneID; 84568358; -.
DR GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR045155; Beta-lactam_cat.
DR InterPro; IPR000871; Beta-lactam_class-A.
DR InterPro; IPR023650; Beta-lactam_class-A_AS.
DR PANTHER; PTHR35333; BETA-LACTAMASE; 1.
DR PANTHER; PTHR35333:SF3; BETA-LACTAMASE2 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance {ECO:0000256|ARBA:ARBA00023251,
KW ECO:0000256|RuleBase:RU361140};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361140};
KW Plasmid {ECO:0000313|EMBL:BAD72947.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..291
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004261573"
FT DOMAIN 49..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 291 AA; 30979 MW; C8DC1D772EAE469E CRC64;
MVTKRVQRMM FAAAACIPLL LGSAPLYAQT SAVQQKLAAL EKSSGGRLGV ALIDTADNTQ
VLYRGDERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTEP TLNTAIPGDP
RDTTTPRAMA QTLRQLTLGH ALGETQRAQL VTWLKGNTTG AASIRAGLPT SWTVGDKTGS
GDYGTTNDIA VIWPQGRAPL VLVTYFTQPQ QNAESRRDVL ASAARIIAEG L
//
