Beta-lactamase TEM
Also known as: bla, blaT-3, blaT-4, blaT-5, blaT-6
Function
TEM-type are the most prevalent beta-lactamases in enterobacteria; they hydrolyze the beta-lactam bond in susceptible beta-lactam antibiotics, thus conferring resistance to penicillins and cephalosporins. TEM-3 and TEM-4 are capable of hydrolyzing cefotaxime and ceftazidime. TEM-5 is capable of hydrolyzing ceftazidime. TEM-6 is capable of hydrolyzing ceftazidime and aztreonam. TEM-8/CAZ-2, TEM-16/CAZ-7 and TEM-24/CAZ-6 are markedly active against ceftazidime. IRT-4 shows resistance to beta-lactamase inhibitors.
Classification
- Family (Pfam)
- PF13354 Beta-lactamase2
- InterPro
- Beta-lactam/transpept-like, Beta-lactam_cat, Beta-lactam_class-A, Beta-lactam_class-A_AS, TEM-12-like
- Functional cluster
- Cell-Envelope & Peptidoglycan Enzymes
Experimental structures · PDB · 78
- 1AXB X-ray 2.00A
- 1BT5 X-ray 1.80A
- 1BTL X-ray 1.80A
- 1CK3 X-ray 2.28A
- 1ERM X-ray 1.70A
- 1ERO X-ray 2.10A
- 1ERQ X-ray 1.90A
- 1ESU X-ray 2.00A
- 1FQG X-ray 1.70A
- 1JTD X-ray 2.30A
- 1JTG X-ray 1.73A
- 1JVJ X-ray 1.73A
- … and 66 more
A predicted model is available from AlphaFold.
Gene Ontology · 3
Drugs targeting this protein · 6
- CLAVULANATE POTASSIUM inhibitor
- SULBACTAM SODIUM inhibitor
- TAZOBACTAM SODIUM inhibitor
- AVIBACTAM SODIUM inhibitor
- RELEBACTAM inhibitor
- ENMETAZOBACTAM inhibitor
Related proteins · sequence + function similarity
- Beta-lactamase TEM-12 1.00
- Beta-lactamase OXY-2 0.89
- Beta-lactamase SHV-1 0.89
- Beta-lactamase SHV-1 0.89
- Beta-lactamase SHV-24 0.89
- Beta-lactamase SHV-6 0.89
- Beta-lactamase SHV-8 0.89
- Beta-lactamase SHV-2 0.89
- Beta-lactamase SHV-2 0.89
- Beta-lactamase SHV-3 0.89
- Beta-lactamase SHV-4 0.89
- Beta-lactamase SHV-13 0.89
Co-cited proteins · studied together in the literature
- Transposon Tn3 resolvase 1 shared papers
- Beta-lactamase inhibitory protein 1 shared papers
- Uncharacterized 15.3 kDa protein 1 shared papers
- Uncharacterized 10.0 kDa protein 1 shared papers
- Uncharacterized 9.4 kDa protein 1 shared papers
- Regulatory protein rop 1 shared papers
- Colicin-E1 immunity protein 1 shared papers
- Tetracycline resistance protein, class C 1 shared papers
- Uncharacterized 9.2 kDa protein 1 shared papers
- Protein CopA/IncA 1 shared papers
- Uncharacterized protein repA4 1 shared papers
- Antitoxin PemI 1 shared papers
Literature · 15 cited papers
- X-ray structure of the Asn276Asp variant of the Escherichia coli TEM-1 beta-lactamase: direct observation of electrostatic modulation in resistance to inactivation by clavulanic acid. Biochemistry · 1999
- Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases. Biochemistry · 1998
- A potent new mode of beta-lactamase inhibition revealed by the 1.7 A X-ray crystallographic structure of the TEM-1-BLIP complex. Nat. Struct. Biol. · 1996
- Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8-A resolution. Proteins · 1993
- Characterization and amino acid sequence of IRT-4, a novel TEM-type enzyme with a decreased susceptibility to beta-lactamase inhibitors. FEMS Microbiol. Lett. · 1994
- DNA replication of the resistance plasmid R100 and its control. Adv. Biophys. · 1986
- Characterization of the plasmid genes blaT-4 and blaT-5 which encode the broad-spectrum beta-lactamases TEM-4 and TEM-5 in enterobacteriaceae. Gene · 1989
- A standard numbering scheme for the class A beta-lactamases. Biochem. J. · 1991
- An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae. J. Gen. Microbiol. · 1991
- Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5-A resolution. FEBS Lett. · 1992
- Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes. Antimicrob. Agents Chemother. · 1992
- A new example of physical linkage between Tn1 and Tn21: the antibiotic multiple-resistance region of plasmid pCFF04 encoding extended-spectrum beta-lactamase TEM-3. Mol. Gen. Genet. · 1992
- … and 3 more in the literature graph
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