ID   BLAT_KLEOX              Reviewed;         286 AA.
AC   Q48406;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=Beta-lactamase TEM-12;
DE            EC=3.5.2.6;
DE   Flags: Precursor;
GN   Name=blaT-12b;
OS   Klebsiella oxytoca.
OG   Plasmid pOZ201.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=571;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION IN RESISTANCE TO
RP   CEFTAZIDIME.
RC   STRAIN=0400-1; PLASMID=pOZ201; TRANSPOSON=Tn841;
RX   PubMed=1329636; DOI=10.1128/aac.36.9.1981;
RA   Heritage J., Hawkey P.M., Todd N., Lewis I.J.;
RT   "Transposition of the gene encoding a TEM-12 extended-spectrum beta-
RT   lactamase.";
RL   Antimicrob. Agents Chemother. 36:1981-1986(1992).
CC   -!- FUNCTION: TEM-type are the most prevalent beta-lactamases in
CC       enterobacteria; they hydrolyze the beta-lactam bond in susceptible
CC       beta-lactam antibiotics, thus conferring resistance to penicillins and
CC       cephalosporins such as ceftazidime. {ECO:0000269|PubMed:1329636}.
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; Evidence={ECO:0000255|PROSITE-
CC         ProRule:PRU10101};
CC   -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC       {ECO:0000305}.
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DR   EMBL; M88143; AAA25053.1; -; Genomic_DNA.
DR   RefSeq; WP_042065300.1; NG_050163.1.
DR   AlphaFoldDB; Q48406; -.
DR   BMRB; Q48406; -.
DR   SMR; Q48406; -.
DR   KEGG; ag:AAA25053; -.
DR   GO; GO:0008800; F:beta-lactamase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030655; P:beta-lactam antibiotic catabolic process; IEA:InterPro.
DR   GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Antibiotic resistance; Disulfide bond; Hydrolase; Plasmid; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..286
FT                   /note="Beta-lactamase TEM-12"
FT                   /id="PRO_0000364051"
FT   ACT_SITE        68
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10101"
FT   ACT_SITE        166
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         232..234
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   DISULFID        75..121
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   286 AA;  31446 MW;  BB6788F3BBA8924B CRC64;
     MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
     EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
     CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DSWEPELNEA IPNDERDTTM
     PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS
     RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW
//