ID   B1PDJ7_ECOLX            Unreviewed;       271 AA.
AC   B1PDJ7;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 47.
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;
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ABY86753.1};
RN   [1] {ECO:0000313|EMBL:ABY86753.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=SB3/1 {ECO:0000313|EMBL:ABY86753.1};
RA   Kmet V.;
RT   "First report of the calf Escherichia coli strain producing CTX-M1 in
RT   Slovakia.";
RL   Submitted (JAN-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|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; EU401703; ABY86753.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1PDJ7; -.
DR   MEROPS; S11.A01; -.
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}.
FT   DOMAIN          30..244
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABY86753.1"
FT   NON_TER         271
FT                   /evidence="ECO:0000313|EMBL:ABY86753.1"
SQ   SEQUENCE   271 AA;  29011 MW;  997D165044CC069F CRC64;
     LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ ILYRADERFA MCSTSKVMAV
     AAVLKKSESE PNLLNQRVEI KKSDLVNYNP IAEKHVDGTM SLAELSAAAL QYSDNVAMNK
     LISHVGGPAS VTAFARQLGD ETFRLDRTEP TLNTAIPGDP RDTTSPRAMA QTLRNLTLGK
     ALGDSQRAQL VTWMKGNTTG AASIQAGLPA SWVVGDKTGS GDYGTTNDIA VIWPKDRAPL
     ILVTYFTQPQ PKAESRRDVL ASAAKIVTNG L
//