ID Q5MDG6_ECOLX Unreviewed; 221 AA.
AC Q5MDG6;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 68.
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=tem {ECO:0000313|EMBL:AAV91693.1};
OS Escherichia coli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:AAV91693.1};
RN [1] {ECO:0000313|EMBL:AAV91693.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=028 {ECO:0000313|EMBL:AAV91692.1}, 145
RC {ECO:0000313|EMBL:AAV91694.1}, and 157 {ECO:0000313|EMBL:AAV91693.1};
RX PubMed=15814998; DOI=10.1128/JCM.43.4.1776-1781.2005;
RA Nemoy L.L., Kotetishvili M., Tigno J., Keefer-Norris A., Harris A.D.,
RA Perencevich E.N., Johnson J.A., Torpey D., Sulakvelidze A., Morris J.G. Jr,
RA Stine O.C.;
RT "Multilocus sequence typing versus pulsed-field gel electrophoresis for
RT characterization of extended-spectrum beta-lactamase-producing Escherichia
RT coli isolates.";
RL J. Clin. Microbiol. 43:1776-1781(2005).
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; AY832931; AAV91692.1; -; Genomic_DNA.
DR EMBL; AY832932; AAV91693.1; -; Genomic_DNA.
DR EMBL; AY832933; AAV91694.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5MDG6; -.
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};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..221
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007706142"
FT DOMAIN 48..215
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
FT NON_TER 221
FT /evidence="ECO:0000313|EMBL:AAV91693.1"
SQ SEQUENCE 221 AA; 24669 MW; 8618BA0941A37AEA CRC64;
MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR S
//
