ID   C8BX39_ENTCL            Unreviewed;       291 AA.
AC   C8BX39;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   27-MAR-2024, entry version 48.
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=blaCTX-M-64 {ECO:0000313|EMBL:ACU87985.1};
OS   Enterobacter cloacae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter; Enterobacter cloacae complex.
OX   NCBI_TaxID=550 {ECO:0000313|EMBL:ACU87985.1};
RN   [1] {ECO:0000313|EMBL:ACU87985.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=0161W {ECO:0000313|EMBL:ACU87985.1};
RA   Sun Y., Zeng Z., Chen S., Ma J., He L., Liu Y., Deng Y., Lei T., Zhao J.,
RA   Liu J.-H.;
RT   "High prevalence of blaCTX-M extended-spectrum beta-lactamase genes in
RT   Escherichia coli isolates from pets and emergence of CTX-M-64 in China.";
RL   Clin. Microbiol. Infect. 16:1475-1481(2010).
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; GQ300937; ACU87985.1; -; Genomic_DNA.
DR   AlphaFoldDB; C8BX39; -.
DR   SMR; C8BX39; -.
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..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..291
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002989354"
FT   DOMAIN          50..264
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
SQ   SEQUENCE   291 AA;  31117 MW;  C5BDFD65DCCEB026 CRC64;
     MVKKSLRQFT LMATATVTLL LGSVPLYAQT ADVQQKLAEL ERQSGGRLGV ALINTADNSQ
     ILYRADERFP MCSTSKVMAA AAVLKQSETQ KQLLNQPVEI KPADLVNYNP IAEKHVNGTM
     TLAELSAAAL QYSDNTAMNK LIAQLGGPGG VTAFARAIGD ETFRLDRTEP TLNTAIPGDP
     RDTTTPRAMA QTLRQLTLGH ALGETQRAQL VTWLKGNTTG AASIRAGLPA SWVVGDKTGS
     GGYGTTNDIA VIWPKDRAPL ILVTYFTQPQ PKAESRRDVL ASAAKIVTDG L
//