ID   I6Z9G4_ECOLX            Unreviewed;       277 AA.
AC   I6Z9G4;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=CTX-M {ECO:0000313|EMBL:AFN66247.1};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:AFN66247.1};
RN   [1] {ECO:0000313|EMBL:AFN66247.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=FC 7116 {ECO:0000313|EMBL:AFN66247.1};
RA   Xu X.;
RT   "Characterization of cefotaxime and ciprofloxacin co-resistant Escherichia
RT   coli isolates in retailed chicken carcasses and ground pork, China.";
RL   Submitted (JUN-2012) 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; JX206416; AFN66247.1; -; Genomic_DNA.
DR   AlphaFoldDB; I6Z9G4; -.
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..277
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003706946"
FT   DOMAIN          42..257
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:AFN66247.1"
FT   NON_TER         277
FT                   /evidence="ECO:0000313|EMBL:AFN66247.1"
SQ   SEQUENCE   277 AA;  29367 MW;  1C325331BD50C8C4 CRC64;
     RMMFAAAACI PLLLGSAPLY AQTSAVQQKL AALEKSSGGR LGVALIDTAD NTQVLYRGDE
     RFPMCSTSKV MAAAAVLKQS ETQKQLPNQP VEIKPADLVN YNPIAEKHVN GTMTLAELSA
     AALQYSDNTA MNKLIAQLGG PGGVTAFARA IGDETFRLDR TEPTLNTAIP GDPRDTTTPR
     AMAQTLRQLT LGHALGETQR AQLVTWLKGN TTGAASIRAG LPTSWTVGDK TGSGDYGTTN
     DIAVIWPQGR APLVLVTYFT QPQQNAESRR DVLASAA
//