ID D1LDK9_ECOLX Unreviewed; 272 AA.
AC D1LDK9;
DT 19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT 19-JAN-2010, sequence version 1.
DT 27-MAR-2024, entry version 40.
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};
DE Flags: Fragment;
GN Name=blaCTX-M-9 {ECO:0000313|EMBL:ACZ16614.1};
OS Escherichia coli.
OG Plasmid pRYC110-Fec245 {ECO:0000313|EMBL:ACZ16614.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:ACZ16614.1};
RN [1] {ECO:0000313|EMBL:ACZ16614.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Fec245 {ECO:0000313|EMBL:ACZ16614.1};
RC PLASMID=pRYC110-Fec245 {ECO:0000313|EMBL:ACZ16614.1};
RX PubMed=19786598; DOI=10.1128/AAC.01706-08;
RA Valverde A., Canton R., Garcillan-Barcia M.P., Novais A., Galan J.C.,
RA Alvarado A., de la Cruz F., Baquero F., Coque T.M.;
RT "Spread of bla(CTX-M-14) is driven mainly by IncK plasmids disseminated
RT among Escherichia coli phylogroups A, B1, and D in Spain.";
RL Antimicrob. Agents Chemother. 53:5204-5212(2009).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; GQ892050; ACZ16614.1; -; Genomic_DNA.
DR AlphaFoldDB; D1LDK9; -.
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:ACZ16614.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 29..272
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003024116"
FT DOMAIN 49..264
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 272
FT /evidence="ECO:0000313|EMBL:ACZ16614.1"
SQ SEQUENCE 272 AA; 28971 MW; 2AF823663FEB7E5A CRC64;
MVTKRVQRMM FAAAACIPLL LGSAPLYAQT SAVQQKLAAL EKSSGGRLGV ALIDTADNTQ
VLYRGDERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTEP TLNTAIPGDP
RDTTTPRAMA QTLRQLTLGH ALGETQRAQL VTWLKGNTTG AASIRAGLPT SWTAGDKTGS
GDYGTTNDIA VIWPQGRAPL VLVTYFTQPQ QN
//
