ID   Q1WBU1_ECOLX            Unreviewed;       277 AA.
AC   Q1WBU1;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 58.
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;
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562 {ECO:0000313|EMBL:ABD93868.1};
RN   [1] {ECO:0000313|EMBL:ABD93868.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=987 {ECO:0000313|EMBL:ABD93868.1};
RA   Palasubramaniam S.;
RT   "SHV-12 ESBL producing E. coli.";
RL   Submitted (FEB-2006) 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ408261; ABD93868.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1WBU1; -.
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..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..277
FT                   /note="Beta-lactamase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004197261"
FT   DOMAIN          43..256
FT                   /note="Beta-lactamase class A catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF13354"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:ABD93868.1"
FT   NON_TER         277
FT                   /evidence="ECO:0000313|EMBL:ABD93868.1"
SQ   SEQUENCE   277 AA;  30012 MW;  24F20FDA8A3FE1D7 CRC64;
     WVIFPIISLL ATLPLAVHAS PQPLEQIKQS ESQLSGRVGM IEMDLASGRT LTAWRADERF
     PMMSTFKVVL CGAVLARVDA GDEQLERKIH YRQQDLVDYS PVSEKHLADG MTVGELCAAA
     ITMSDNSAAN LLLATVGGPA GLTAFLRQIG DNVTRLDRWE TELNEALPGD ARDTTTPASM
     AATLRKLLTS QRLSARSQRQ LLQWMVDDRV AGPLIRSVLP AGWFIADKTG ASKRGARGIV
     ALLGPNNKAE RIVVIYLRDT PASMAERNQQ IAGIGAA
//