ID M5B5Q1_ECOLX Unreviewed; 286 AA.
AC M5B5Q1;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=blaTEM-184 {ECO:0000313|EMBL:CCA61905.1};
OS Escherichia coli.
OG Plasmid pCT-1 {ECO:0000313|EMBL:CCA61905.1}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562 {ECO:0000313|EMBL:CCA61905.1};
RN [1] {ECO:0000313|EMBL:CCA61905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PI-12197 {ECO:0000313|EMBL:CCA61905.1};
RC PLASMID=pCT-1 {ECO:0000313|EMBL:CCA61905.1};
RA D'Andrea M.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCA61905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=PI-12197 {ECO:0000313|EMBL:CCA61905.1};
RC PLASMID=pCT-1 {ECO:0000313|EMBL:CCA61905.1};
RA Giani T., D'Andrea M.M., Leonildi A., Menichetti F., Tascini C.,
RA Rossolini G.M.;
RT "Novel TEM-type extended spectrum beta-lactamase in Escherichia coli
RT isolate from Pisa, Italy.";
RL Submitted (MAR-2013) 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; FR848831; CCA61905.1; -; Genomic_DNA.
DR RefSeq; WP_063864882.1; NG_050221.1.
DR AlphaFoldDB; M5B5Q1; -.
DR SMR; M5B5Q1; -.
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 Plasmid {ECO:0000313|EMBL:CCA61905.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..286
FT /note="Beta-lactamase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004063097"
FT DOMAIN 48..261
FT /note="Beta-lactamase class A catalytic"
FT /evidence="ECO:0000259|Pfam:PF13354"
SQ SEQUENCE 286 AA; 31401 MW; 73EB651D9CA031BB CRC64;
MSIKHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VKYSPVTEKH LTDGMTVREL
CSAAVTMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DSWEPELNEA IPNDERDTTT
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS
RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW
//
