ID   B2CR57_ECOLX            Unreviewed;       291 AA.
AC   B2CR57;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-MAR-2024, entry version 55.
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};
OS   Escherichia coli.
OG   Plasmid pKP168 {ECO:0000313|EMBL:ACB41777.1}.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ACB41777.1};
RN   [1] {ECO:0000313|EMBL:ACB41777.1}
RP   NUCLEOTIDE SEQUENCE.
RC   PLASMID=pKP168 {ECO:0000313|EMBL:ACB41777.1};
RA   Yin J., Cheng J., Sun Z., Ye Y., Gao Y.F., Li J.B., Zhang X.J.;
RT   "Characterization of two plasmid-encoded cefotaximases found in clinical
RT   Escherichia coli isolates: CTX-M-65 and a novel enzyme, CTX-M-87.";
RL   J. Med. Microbiol. 58:811-815(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}.
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DR   EMBL; EU545409; ACB41777.1; -; Genomic_DNA.
DR   RefSeq; WP_032492184.1; NG_049040.1.
DR   AlphaFoldDB; B2CR57; -.
DR   SMR; B2CR57; -.
DR   KEGG; ag:ACB41777; -.
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:ACB41777.1}; 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_5002776892"
FT   DOMAIN          49..264
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   291 AA;  31023 MW;  31383C149720C6CA CRC64;
     MVTKRVQRMM FAAAACIPLL LGSAPLYAQT SAVQQKLAAL EKSSGGRLGV ALIDTADNTQ
     VLYRGDERFP MCSTSKVMAV AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
     TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTEL TLNTAIPGDP
     RDTTTPRAMA QTLRQLTLGH ALGETQRAQL VTWLKGNTTG AASIRAGLPT SWTVGDKTGS
     GDYGTTNDIA VIWPQGRAPL VLVTYFTQPQ QNAESRRDVL ASAARIIAEG L
//