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 27-MAR-2024, entry version 148. 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; Pseudomonadota; 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}. 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; 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_032488414.1; NZ_UFZR01000001.1. DR RefSeq; WP_063864949.1; NZ_CP070151.1. 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_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 PDB; 7QLP; X-ray; 2.30 A; A/B/C/D/E/F=24-286. DR PDB; 7QNK; X-ray; 2.50 A; A/B/C/D/E/F=24-286. DR PDB; 7QOR; X-ray; 2.00 A; AAA/BBB/CCC/DDD/EEE/FFF=24-286. DR PDB; 8DDZ; X-ray; 1.45 A; A/B/C/D=24-286. DR PDB; 8DE0; X-ray; 1.72 A; A/B/C/D=24-286. DR PDB; 8DE1; X-ray; 1.56 A; A/B/C/D=24-286. DR PDB; 8DE2; X-ray; 2.45 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 PDBsum; 7QLP; -. DR PDBsum; 7QNK; -. DR PDBsum; 7QOR; -. DR PDBsum; 8DDZ; -. DR PDBsum; 8DE0; -. DR PDBsum; 8DE1; -. DR PDBsum; 8DE2; -. 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 ABCD; P62593; 7 sequenced antibodies. DR GeneID; 84568456; -. 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 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; 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 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:8DE1" 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 //