BLAT_ECOLX
ID BLAT_ECOLX Reviewed; 286 AA.
AC P62593; P00810; Q47313;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Beta-lactamase TEM;
DE EC=3.5.2.6;
DE AltName: Full=IRT-4;
DE AltName: Full=Penicillinase;
DE AltName: Full=TEM-1;
DE AltName: Full=TEM-16/CAZ-7;
DE AltName: Full=TEM-2;
DE AltName: Full=TEM-24/CAZ-6;
DE AltName: Full=TEM-3;
DE AltName: Full=TEM-4;
DE AltName: Full=TEM-5;
DE AltName: Full=TEM-6;
DE AltName: Full=TEM-8/CAZ-2;
DE Flags: Precursor;
GN Name=bla;
GN and
GN Name=blaT-3;
GN and
GN Name=blaT-4;
GN and
GN Name=blaT-5;
GN and
GN Name=blaT-6;
OS Escherichia coli.
OG Plasmid R1 (R7268), Plasmid IncFII R100 (NR1), Plasmid R6K, Plasmid pUD16,
OG Plasmid pCFF04, and Plasmid pCFF14.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
RC PLASMID=R1 (R7268); TRANSPOSON=Tn3;
RX PubMed=358200; DOI=10.1073/pnas.75.8.3737;
RA Sutcliffe J.G.;
RT "Nucleotide sequence of the ampicillin resistance gene of Escherichia coli
RT plasmid pBR322.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:3737-3741(1978).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
RC PLASMID=R1 (R7268); TRANSPOSON=Tn3;
RX PubMed=383387; DOI=10.1101/sqb.1979.043.01.013;
RA Sutcliffe J.G.;
RT "Complete nucleotide sequence of the Escherichia coli plasmid pBR322.";
RL Cold Spring Harb. Symp. Quant. Biol. 43:77-90(1979).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-1).
RC PLASMID=IncFII R100 (NR1);
RX PubMed=3019092; DOI=10.1016/0065-227x(86)90018-3;
RA Ohtsubo H., Ryder T.B., Maeda Y., Armstrong K., Ohtsubo E.;
RT "DNA replication of the resistance plasmid R100 and its control.";
RL Adv. Biophys. 21:115-133(1986).
RN [4]
RP PROTEIN SEQUENCE OF 24-286 (TEM-2).
RC PLASMID=R6K; TRANSPOSON=Tn1;
RX PubMed=358199; DOI=10.1073/pnas.75.8.3732;
RA Ambler R.P., Scott G.K.;
RT "Partial amino acid sequence of penicillinase coded by Escherichia coli
RT plasmid R6K.";
RL Proc. Natl. Acad. Sci. U.S.A. 75:3732-3736(1978).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
RA Sougakoff W., Goussard S., Courvalin P.;
RT "The TEM-3 beta-lactamase, which hydrolyzes broad-spectrum cephalosporins,
RT is derived from the TEM-2 penicillinase by two amino acid substitutions.";
RL FEMS Microbiol. Lett. 56:343-348(1988).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-3).
RC PLASMID=pCFF04;
RX PubMed=1331747; DOI=10.1007/bf00286188;
RA Mabilat C., Lourencao-Vital J., Goussard S., Courvalin P.;
RT "A new example of physical linkage between Tn1 and Tn21: the antibiotic
RT multiple-resistance region of plasmid pCFF04 encoding extended-spectrum
RT beta-lactamase TEM-3.";
RL Mol. Gen. Genet. 235:113-121(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-4 AND TEM-5).
RC STRAIN=CB86134; PLASMID=pCFF04, and pUD16;
RX PubMed=2550326; DOI=10.1016/0378-1119(89)90236-9;
RA Sougakoff W., Petit A., Goussard S., Sirot D., Bure A., Courvalin P.;
RT "Characterization of the plasmid genes blaT-4 and blaT-5 which encode the
RT broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae.";
RL Gene 78:339-348(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-6).
RC STRAIN=HB251;
RX PubMed=1665171; DOI=10.1099/00221287-137-12-2681;
RA Goussard S., Sougakoff W., Mabilat C., Bauernfeind A., Courvalin P.;
RT "An IS1-like element is responsible for high-level synthesis of extended-
RT spectrum beta-lactamase TEM-6 in Enterobacteriaceae.";
RL J. Gen. Microbiol. 137:2681-2687(1991).
RN [9]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (TEM-8; TEM-16 AND TEM-24).
RX PubMed=1416873; DOI=10.1128/aac.36.9.1817;
RA Chanal C., Poupart M.C., Sirot D., Labia R., Sirot J., Cluzel R.;
RT "Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes.";
RL Antimicrob. Agents Chemother. 36:1817-1820(1992).
RN [10]
RP PROTEIN SEQUENCE OF 24-286 (IRT-4).
RC STRAIN=PEY;
RX PubMed=8056282; DOI=10.1111/j.1574-6968.1994.tb07016.x;
RA Brun T., Peduzzi J., Canica M.M., Paul G., Nevot P., Barthelemy M.,
RA Labia R.;
RT "Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme
RT with a decreased susceptibility to beta-lactamase inhibitors.";
RL FEMS Microbiol. Lett. 120:111-117(1994).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF TEM-1.
RX PubMed=1544485; DOI=10.1016/0014-5793(92)80232-6;
RA Jelsch C., Lenfant F., Masson J.-M., Samama J.-P.;
RT "Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A
RT resolution.";
RL FEBS Lett. 299:135-142(1992).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF TEM-1.
RX PubMed=8356032; DOI=10.1002/prot.340160406;
RA Jelsch C., Mourey L., Masson J.-M., Samama J.-P.;
RT "Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A
RT resolution.";
RL Proteins 16:364-383(1993).
RN [13]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF TEM-1 COMPLEXED WITH BLIP.
RX PubMed=8605632; DOI=10.1038/nsb0396-290;
RA Strynadka N.C.J., Jensen S.E., Alzari P.M., James M.N.G.;
RT "A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray
RT crystallographic structure of the TEM-1-BLIP complex.";
RL Nat. Struct. Biol. 3:290-297(1996).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF TEM-1.
RX PubMed=9485412; DOI=10.1021/bi972501b;
RA Maveyraud L., Pratt R.F., Samama J.-P.;
RT "Crystal structure of an acylation transition-state analog of the TEM-1
RT beta-lactamase. Mechanistic implications for class A beta-lactamases.";
RL Biochemistry 37:2622-2628(1998).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF TEM-1.
RX PubMed=10423234; DOI=10.1021/bi990758z;
RA Swaren P., Golemi D., Cabantous S., Bulychev A., Maveyraud L.,
RA Mobashery S., Samama J.-P.;
RT "X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1
RT beta-lactamase: direct observation of electrostatic modulation in
RT resistance to inactivation by clavulanic acid.";
RL Biochemistry 38:9570-9576(1999).
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. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime
CC and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is
CC capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-
CC 16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-
CC 4 shows resistance to beta-lactamase inhibitors.
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 -!- INTERACTION:
CC P62593; P35804; Xeno; NbExp=2; IntAct=EBI-1031989, EBI-1031985;
CC -!- BIOTECHNOLOGY: This protein is used as a marker in many commonly used
CC cloning vectors, such as pBR322 and the pUC series.
CC -!- MISCELLANEOUS: The beta-lactamase present on pBR322 was cloned from
CC plasmid R1 (R7268).
CC -!- SIMILARITY: Belongs to the class-A beta-lactamase family.
CC {ECO:0000305}.
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DR EMBL; J01749; AAB59737.1; -; Genomic_DNA.
DR EMBL; V00613; CAA23886.1; -; Genomic_DNA.
DR EMBL; X64523; CAA45828.1; -; Genomic_DNA.
DR EMBL; X57972; CAA41038.1; -; Genomic_DNA.
DR EMBL; X65252; CAA46344.1; -; Genomic_DNA.
DR EMBL; X65253; CAA46345.1; -; Genomic_DNA.
DR EMBL; X65254; CAA46346.1; -; Genomic_DNA.
DR EMBL; U89928; AAB64386.1; -; Genomic_DNA.
DR EMBL; U66885; AAC48875.1; -; Genomic_DNA.
DR PIR; A93821; PNECP.
DR PIR; S30113; S30113.
DR RefSeq; NP_943295.1; NC_005248.1.
DR RefSeq; NP_957565.1; NC_005327.1.
DR RefSeq; WP_000027057.1; NZ_WWEL01000113.1.
DR RefSeq; WP_063864949.1; NZ_BGKM01000047.1.
DR RefSeq; WP_063865014.1; NZ_BGLS01000178.1.
DR RefSeq; YP_001096393.1; NC_009132.1.
DR RefSeq; YP_001693174.1; NC_010378.1.
DR RefSeq; YP_001816609.1; NC_010558.1.
DR RefSeq; YP_003108102.1; NC_013120.1.
DR RefSeq; YP_003108210.1; NC_013121.1.
DR RefSeq; YP_003829069.1; NC_014383.1.
DR RefSeq; YP_003829170.1; NC_014384.1.
DR RefSeq; YP_003937675.1; NC_014615.1.
DR RefSeq; YP_004119720.1; NC_014843.1.
DR RefSeq; YP_004119734.1; NC_014843.1.
DR RefSeq; YP_006903139.1; NC_019047.1.
DR RefSeq; YP_006939984.1; NC_018994.1.
DR RefSeq; YP_006940092.1; NC_018995.1.
DR RefSeq; YP_006952181.1; NC_019056.1.
DR RefSeq; YP_006952421.1; NC_019062.1.
DR RefSeq; YP_006952427.1; NC_019063.1.
DR RefSeq; YP_006953479.1; NC_019073.1.
DR RefSeq; YP_006953762.1; NC_019088.1.
DR RefSeq; YP_006953988.1; NC_019091.1.
DR RefSeq; YP_006954235.1; NC_019095.1.
DR RefSeq; YP_007447512.1; NC_020278.2.
DR RefSeq; YP_008864019.1; NC_022992.1.
DR RefSeq; YP_008864686.1; NC_022996.1.
DR RefSeq; YP_008995211.1; NC_023277.2.
DR RefSeq; YP_009060387.1; NC_024960.1.
DR RefSeq; YP_009060444.1; NC_024961.1.
DR RefSeq; YP_009060580.1; NC_024967.1.
DR RefSeq; YP_009061316.1; NC_024977.1.
DR RefSeq; YP_009066523.1; NC_025106.1.
DR RefSeq; YP_009068284.1; NC_025139.1.
DR RefSeq; YP_009068507.1; NC_025141.1.
DR RefSeq; YP_009070232.1; NC_025167.1.
DR RefSeq; YP_009070558.1; NC_025175.1.
DR RefSeq; YP_009071512.1; NC_025183.1.
DR RefSeq; YP_190222.1; NC_006671.1.
DR PDB; 1AXB; X-ray; 2.00 A; A=24-286.
DR PDB; 1BT5; X-ray; 1.80 A; A=24-286.
DR PDB; 1BTL; X-ray; 1.80 A; A=24-286.
DR PDB; 1CK3; X-ray; 2.28 A; A=24-284.
DR PDB; 1ERM; X-ray; 1.70 A; A=24-286.
DR PDB; 1ERO; X-ray; 2.10 A; A=24-286.
DR PDB; 1ERQ; X-ray; 1.90 A; A=24-286.
DR PDB; 1ESU; X-ray; 2.00 A; A=24-284.
DR PDB; 1FQG; X-ray; 1.70 A; A=24-286.
DR PDB; 1JTD; X-ray; 2.30 A; A=24-286.
DR PDB; 1JTG; X-ray; 1.73 A; A/C=24-286.
DR PDB; 1JVJ; X-ray; 1.73 A; A=24-286.
DR PDB; 1JWP; X-ray; 1.75 A; A=24-286.
DR PDB; 1JWV; X-ray; 1.85 A; A=24-286.
DR PDB; 1JWZ; X-ray; 1.80 A; A=24-286.
DR PDB; 1LHY; X-ray; 2.00 A; A=24-284.
DR PDB; 1LI0; X-ray; 1.61 A; A=24-284.
DR PDB; 1LI9; X-ray; 1.52 A; A=24-284.
DR PDB; 1M40; X-ray; 0.85 A; A=24-286.
DR PDB; 1NXY; X-ray; 1.60 A; A=24-286.
DR PDB; 1NY0; X-ray; 1.75 A; A=24-286.
DR PDB; 1NYM; X-ray; 1.20 A; A=24-286.
DR PDB; 1NYY; X-ray; 1.90 A; A=24-286.
DR PDB; 1PZO; X-ray; 1.90 A; A=24-284.
DR PDB; 1PZP; X-ray; 1.45 A; A=24-284.
DR PDB; 1S0W; X-ray; 2.30 A; A/B=24-286.
DR PDB; 1TEM; X-ray; 1.95 A; A=24-286.
DR PDB; 1XPB; X-ray; 1.90 A; A=24-286.
DR PDB; 1XXM; X-ray; 1.90 A; A/B=24-286.
DR PDB; 1YT4; X-ray; 1.40 A; A=24-284.
DR PDB; 1ZG4; X-ray; 1.55 A; A=1-284.
DR PDB; 1ZG6; X-ray; 2.10 A; A=1-284.
DR PDB; 2B5R; X-ray; 1.65 A; A/B=24-286.
DR PDB; 2V1Z; X-ray; 1.60 A; A=25-38, A=41-286.
DR PDB; 2V20; X-ray; 1.67 A; A=25-38, A=41-286.
DR PDB; 3C7U; X-ray; 2.20 A; A/C=24-286.
DR PDB; 3C7V; X-ray; 2.07 A; A/C=24-286.
DR PDB; 3CMZ; X-ray; 1.92 A; A=24-286.
DR PDB; 3DTM; X-ray; 2.00 A; A=24-286.
DR PDB; 3JYI; X-ray; 2.70 A; A/B/C/D/E/F=24-286.
DR PDB; 3TOI; X-ray; 1.90 A; A/B=39-283.
DR PDB; 4DXB; X-ray; 2.29 A; A/B=24-226.
DR PDB; 4DXC; X-ray; 2.30 A; A=24-226.
DR PDB; 4GKU; X-ray; 1.92 A; A=24-286.
DR PDB; 4IBR; X-ray; 2.20 A; A=24-286.
DR PDB; 4IBX; X-ray; 2.68 A; A/B/C/D/E=24-286.
DR PDB; 4ID4; X-ray; 1.05 A; A=24-147, A=189-286.
DR PDB; 4MEZ; X-ray; 2.05 A; A/B=24-286.
DR PDB; 4QY5; X-ray; 1.50 A; A=24-147, A=189-286.
DR PDB; 4QY6; X-ray; 1.15 A; A=24-147, A=189-286.
DR PDB; 4R4R; X-ray; 1.20 A; A=24-147, A=189-286.
DR PDB; 4R4S; X-ray; 1.10 A; A=24-149, A=189-286.
DR PDB; 4RVA; X-ray; 1.44 A; A=24-286.
DR PDB; 4RX2; X-ray; 2.31 A; A/B/C/D/E/F/G/H=24-286.
DR PDB; 4RX3; X-ray; 1.39 A; A=24-286.
DR PDB; 4ZJ1; X-ray; 1.54 A; A=1-286.
DR PDB; 4ZJ2; X-ray; 1.80 A; A=1-286.
DR PDB; 4ZJ3; X-ray; 1.70 A; A=1-286.
DR PDB; 5HVI; X-ray; 1.64 A; A/B/C/D=24-286.
DR PDB; 5HW1; X-ray; 1.70 A; A/B/C/D=24-286.
DR PDB; 5HW5; X-ray; 1.41 A; A/B/C/D=24-286.
DR PDB; 5I52; X-ray; 1.75 A; A/B/C/D=24-286.
DR PDB; 5I63; X-ray; 1.95 A; A/B/C/D=24-286.
DR PDB; 5IQ8; X-ray; 2.06 A; A/B/C/D=24-286.
DR PDB; 5KKF; X-ray; 1.82 A; A/B/C/D=24-286.
DR PDB; 5KPU; X-ray; 1.50 A; A/B/C/D=24-286.
DR PDB; 5NPO; X-ray; 1.95 A; A=24-286.
DR PDB; 6APA; X-ray; 1.86 A; A/B/C/D=24-286.
DR PDB; 6AYK; X-ray; 1.44 A; A/B/C/D=24-286.
DR PDB; 6B2N; X-ray; 2.00 A; A/B/C/D=24-286.
DR PDBsum; 1AXB; -.
DR PDBsum; 1BT5; -.
DR PDBsum; 1BTL; -.
DR PDBsum; 1CK3; -.
DR PDBsum; 1ERM; -.
DR PDBsum; 1ERO; -.
DR PDBsum; 1ERQ; -.
DR PDBsum; 1ESU; -.
DR PDBsum; 1FQG; -.
DR PDBsum; 1JTD; -.
DR PDBsum; 1JTG; -.
DR PDBsum; 1JVJ; -.
DR PDBsum; 1JWP; -.
DR PDBsum; 1JWV; -.
DR PDBsum; 1JWZ; -.
DR PDBsum; 1LHY; -.
DR PDBsum; 1LI0; -.
DR PDBsum; 1LI9; -.
DR PDBsum; 1M40; -.
DR PDBsum; 1NXY; -.
DR PDBsum; 1NY0; -.
DR PDBsum; 1NYM; -.
DR PDBsum; 1NYY; -.
DR PDBsum; 1PZO; -.
DR PDBsum; 1PZP; -.
DR PDBsum; 1S0W; -.
DR PDBsum; 1TEM; -.
DR PDBsum; 1XPB; -.
DR PDBsum; 1XXM; -.
DR PDBsum; 1YT4; -.
DR PDBsum; 1ZG4; -.
DR PDBsum; 1ZG6; -.
DR PDBsum; 2B5R; -.
DR PDBsum; 2V1Z; -.
DR PDBsum; 2V20; -.
DR PDBsum; 3C7U; -.
DR PDBsum; 3C7V; -.
DR PDBsum; 3CMZ; -.
DR PDBsum; 3DTM; -.
DR PDBsum; 3JYI; -.
DR PDBsum; 3TOI; -.
DR PDBsum; 4DXB; -.
DR PDBsum; 4DXC; -.
DR PDBsum; 4GKU; -.
DR PDBsum; 4IBR; -.
DR PDBsum; 4IBX; -.
DR PDBsum; 4ID4; -.
DR PDBsum; 4MEZ; -.
DR PDBsum; 4QY5; -.
DR PDBsum; 4QY6; -.
DR PDBsum; 4R4R; -.
DR PDBsum; 4R4S; -.
DR PDBsum; 4RVA; -.
DR PDBsum; 4RX2; -.
DR PDBsum; 4RX3; -.
DR PDBsum; 4ZJ1; -.
DR PDBsum; 4ZJ2; -.
DR PDBsum; 4ZJ3; -.
DR PDBsum; 5HVI; -.
DR PDBsum; 5HW1; -.
DR PDBsum; 5HW5; -.
DR PDBsum; 5I52; -.
DR PDBsum; 5I63; -.
DR PDBsum; 5IQ8; -.
DR PDBsum; 5KKF; -.
DR PDBsum; 5KPU; -.
DR PDBsum; 5NPO; -.
DR PDBsum; 6APA; -.
DR PDBsum; 6AYK; -.
DR PDBsum; 6B2N; -.
DR AlphaFoldDB; P62593; -.
DR BMRB; P62593; -.
DR SMR; P62593; -.
DR IntAct; P62593; 1.
DR BindingDB; P62593; -.
DR ChEMBL; CHEMBL2065; -.
DR ChEMBL; CHEMBL2364670; -.
DR DrugBank; DB07466; (1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACID.
DR DrugBank; DB07464; 1(R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACID.
DR DrugBank; DB02614; 1(R)-1-Acetamido-2-(3-Carboxyphenyl)Ethyl Boronic Acid.
DR DrugBank; DB04430; 3-(4-Phenylamino-Phenylamino)-2-(1h-Tetrazol-5-Yl)-Acrylonitrile.
DR DrugBank; DB08551; 3-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acid.
DR DrugBank; DB07599; [(2-AMINO-ALPHA-METHOXYIMINO-4-THIAZOLYLACETYL)AMINO]METHYLBORONIC ACID.
DR DrugBank; DB02841; [(2-Ethoxy-1-Naphthoyl)Amino]Methylboronic Acid.
DR DrugBank; DB02642; [[N-(Benzyloxycarbonyl)Amino]Methyl]Phosphate.
DR DrugBank; DB09060; Avibactam.
DR DrugBank; DB01053; Benzylpenicillin.
DR DrugBank; DB04035; Ceftazidime BATSI.
DR DrugBank; DB01598; Imipenem.
DR DrugBank; DB04037; N,N-Bis(4-Chlorobenzyl)-1h-1,2,3,4-Tetraazol-5-Amine.
DR DrugBank; DB12377; Relebactam.
DR DrugBank; DB12107; Vaborbactam.
DR DrugCentral; P62593; -.
DR PRIDE; P62593; -.
DR ABCD; P62593; 7 sequenced antibodies.
DR GeneID; 67514328; -.
DR KEGG; ag:AAB59737; -.
DR KEGG; ag:CAA41038; -.
DR KEGG; ag:CAA45828; -.
DR KEGG; ag:CAA46344; -.
DR KEGG; ag:CAA46345; -.
DR KEGG; ag:CAA46346; -.
DR OMA; EWMKGNA; -.
DR OrthoDB; 991474at2; -.
DR BRENDA; 3.5.2.6; 2026.
DR SABIO-RK; P62593; -.
DR EvolutionaryTrace; P62593; -.
DR PRO; PR:P62593; -.
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; -; 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; PTHR35333; 1.
DR Pfam; PF13354; Beta-lactamase2; 1.
DR PRINTS; PR00118; BLACTAMASEA.
DR SUPFAM; SSF56601; SSF56601; 1.
DR PROSITE; PS00146; BETA_LACTAMASE_A; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; Direct protein sequencing;
KW Disulfide bond; Hydrolase; Plasmid; Signal; Transposable element.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:358199,
FT ECO:0000269|PubMed:8056282"
FT CHAIN 24..286
FT /note="Beta-lactamase TEM"
FT /id="PRO_0000016978"
FT ACT_SITE 68
FT /note="Acyl-ester intermediate"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT BINDING 232..234
FT /ligand="substrate"
FT DISULFID 75..121
FT VARIANT 19
FT /note="L -> F (in TEM-4)"
FT VARIANT 37
FT /note="Q -> K (in TEM-2, TEM-3, TEM-8, TEM-16 and TEM-24)"
FT VARIANT 67
FT /note="M -> L (in IRT-4)"
FT VARIANT 102
FT /note="E -> K (in TEM-3, TEM-4, TEM-6, TEM-8, TEM-16 and
FT TEM-24)"
FT VARIANT 162
FT /note="R -> H (in TEM-6 and TEM-16)"
FT VARIANT 162
FT /note="R -> S (in TEM-5, TEM-8 and TEM-24)"
FT VARIANT 235
FT /note="A -> T (in TEM-5 and TEM-24)"
FT VARIANT 236
FT /note="G -> S (in TEM-3, TEM-4 and TEM-8)"
FT VARIANT 237
FT /note="E -> K (in TEM-5 and TEM-24)"
FT VARIANT 261
FT /note="T -> M (in TEM-4)"
FT VARIANT 272
FT /note="N -> D (in IRT-4)"
FT HELIX 25..38
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 40..48
FT /evidence="ECO:0007829|PDB:1M40"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 70..83
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 97..99
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:1M40"
FT TURN 111..113
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 117..126
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 130..139
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 143..152
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:1M40"
FT TURN 171..173
FT /evidence="ECO:0007829|PDB:1JWZ"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:4RX3"
FT HELIX 199..210
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1PZP"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:1M40"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 228..235
FT /evidence="ECO:0007829|PDB:1M40"
FT TURN 237..239
FT /evidence="ECO:0007829|PDB:6APA"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 255..263
FT /evidence="ECO:0007829|PDB:1M40"
FT STRAND 264..266
FT /evidence="ECO:0007829|PDB:4DXB"
FT HELIX 268..284
FT /evidence="ECO:0007829|PDB:1M40"
SQ SEQUENCE 286 AA; 31515 MW; BB678943BB18934B CRC64;
MSIQHFRVAL IPFFAAFCLP VFAHPETLVK VKDAEDQLGA RVGYIELDLN SGKILESFRP
EERFPMMSTF KVLLCGAVLS RVDAGQEQLG RRIHYSQNDL VEYSPVTEKH LTDGMTVREL
CSAAITMSDN TAANLLLTTI GGPKELTAFL HNMGDHVTRL DRWEPELNEA IPNDERDTTM
PAAMATTLRK LLTGELLTLA SRQQLIDWME ADKVAGPLLR SALPAGWFIA DKSGAGERGS
RGIIAALGPD GKPSRIVVIY TTGSQATMDE RNRQIAEIGA SLIKHW
