Beta-lactamase TEM
Details
- Name
- Beta-lactamase TEM
- Kind
- protein
- Synonyms
- 3.5.2.6
- IRT-4
- Penicillinase
- TEM-1
- TEM-16/CAZ-7
- TEM-2
- TEM-24/CAZ-6
- TEM-3
- TEM-4
- TEM-5
- TEM-6
- TEM-8/CAZ-2
- Gene Name
- bla
- UniProtKB Entry
- P62593Swiss-Prot
- Organism
- Escherichia coli
- NCBI Taxonomy ID
- 562
- Amino acid sequence
>lcl|BSEQ0022085|Beta-lactamase TEM MSIQHFRVALIPFFAAFCLPVFAHPETLVKVKDAEDQLGARVGYIELDLNSGKILESFRP EERFPMMSTFKVLLCGAVLSRVDAGQEQLGRRIHYSQNDLVEYSPVTEKHLTDGMTVREL CSAAITMSDNTAANLLLTTIGGPKELTAFLHNMGDHVTRLDRWEPELNEAIPNDERDTTM PAAMATTLRKLLTGELLTLASRQQLIDWMEADKVAGPLLRSALPAGWFIADKSGAGERGS RGIIAALGPDGKPSRIVVIYTTGSQATMDERNRQIAEIGASLIKHW
- Number of residues
- 286
- Molecular Weight
- 31514.865
- Theoretical pI
- 5.92
- GO Classification
- Functionsbeta-lactamase activityProcessesbeta-lactam antibiotic catabolic process / response to antibiotic
- General 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.
- Specific Function
- beta-lactamase activity
- Pfam Domain Function
- Beta-lactamase (PF00144)
- Signal Regions
- 1-23
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0007458|1191 bp ATGAAATCTAACAATGCGCTCATCGTCATCCTCGGCACCGTCACCCTGGATGCTGTAGGC ATAGGCTTGGTTATGCCGGTACTGCCGGGCCTCTTGCGGGATATCGTCCATTCCGACAGC ATCGCCAGTCACTATGGCGTGCTGCTAGCGCTATATGCGTTGATGCAATTTCTATGCGCA CCCGTTCTCGGAGCACTGTCCGACCGCTTTGGCCGCCGCCCAGTCCTGCTCGCTTCGCTA CTTGGAGCCACTATCGACTACGCGATCATGGCGACCACACCCGTCCTGTGGATCCTCTAC GCCGGACGCATCGTGGCCGGCATCACCGGCGCCACAGGTGCGGTTGCTGGCGCCTATATC GCCGACATCACCGATGGGGAAGATCGGGCTCGCCACTTCGGGCTCATGAGCGCTTGTTTC GGCGTGGGTATGGTGGCAGGCCCCGTGGCCGGGGGACTGTTGGGCGCCATCTCCTTGCAT GCACCATTCCTTGCGGCGGCGGTGCTCAACGGCCTCAACCTACTACTGGGCTGCTTCCTA ATGCAGGAGTCGCATAAGGGAGAGCGTCGACCGATGCCCTTGAGAGCCTTCAACCCAGTC AGCTCCTTCCGGTGGGCGCGGGGCATGACTATCGTCGCCGCACTTATGACTGTCTTCTTT ATCATGCAACTCGTAGGACAGGTGCCGGCAGCGCTCTGGGTCATTTTCGGCGAGGACCGC TTTCGCTGGAGCGCGACGATGATCGGCCTGTCGCTTGCGGTATTCGGAATCTTGCACGCC CTCGCTCAAGCCTTCGTCACTGGTCCCGCCACCAAACGTTTCGGCGAGAAGCAGGCCATT ATCGCCGGCATGGCGGCCGACGCGCTGGGCTACGTCTTGCTGGCGTTCGCGACGCGAGGC TGGATGGCCTTCCCCATTATGATTCTTCTCGCTTCCGGCGGCATCGGGATGCCCGCGTTG CAGGCCATGCTGTCCAGGCAGGTAGATGACGACCATCAGGGACAGCTTCAAGGATCGCTC GCGGCTCTTACCAGCCTAACTTCGATCACTGGACCGCTGATCGTCACGGCGATTTATGCC GCCTCGGCGAGCACATGGAACGGGTTGGCATGGATTGTAGGCGCCGCCCTATACCTTGTC TGCCTCCCCGCGTTGCGTCGCGGTGCATGGAGCCGGGCCACCTCGACCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P62593 UniProtKB Entry Name BLAT_ECOLX GenBank Protein ID 208959 GenBank Gene ID J01749 PDB ID(s) 1AXB, 1BT5, 1BTL, 1CK3, 1ERM, 1ERO, 1ERQ, 1ESU, 1FQG, 1JTD, 1JTG, 1JVJ, 1JWP, 1JWV, 1JWZ, 1LHY, 1LI0, 1LI9, 1M40, 1NXY, 1NY0, 1NYM, 1NYY, 1PZO, 1PZP, 1S0W, 1TEM, 1XPB, 1XXM, 1YT4, 1ZG4, 1ZG6, 2B5R, 2V1Z, 2V20, 3C7U, 3C7V, 3CMZ, 3DTM, 3JYI, 3TOI, 4DXB, 4DXC, 4GKU, 4IBR, 4IBX, 4ID4, 4MEZ, 4QY5, 4QY6, 4R4R, 4R4S, 4RVA, 4RX2, 4RX3, 4ZJ1, 4ZJ2, 4ZJ3 KEGG ID ag:AAB59737 NCBI Gene ID 10076131 - General References
- Sutcliffe JG: Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR322. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3737-41. [Article]
- Sutcliffe JG: Complete nucleotide sequence of the Escherichia coli plasmid pBR322. Cold Spring Harb Symp Quant Biol. 1979;43 Pt 1:77-90. [Article]
- Ohtsubo H, Ryder TB, Maeda Y, Armstrong K, Ohtsubo E: DNA replication of the resistance plasmid R100 and its control. Adv Biophys. 1986;21:115-33. [Article]
- Ambler RP, Scott GK: Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K. Proc Natl Acad Sci U S A. 1978 Aug;75(8):3732-6. [Article]
- Mabilat C, Lourencao-Vital J, Goussard S, Courvalin P: 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 Oct;235(1):113-21. [Article]
- Sougakoff W, Petit A, Goussard S, Sirot D, Bure A, Courvalin P: 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 May 30;78(2):339-48. [Article]
- Goussard S, Sougakoff W, Mabilat C, Bauernfeind A, Courvalin P: An IS1-like element is responsible for high-level synthesis of extended-spectrum beta-lactamase TEM-6 in Enterobacteriaceae. J Gen Microbiol. 1991 Dec;137(12):2681-7. [Article]
- Chanal C, Poupart MC, Sirot D, Labia R, Sirot J, Cluzel R: Nucleotide sequences of CAZ-2, CAZ-6, and CAZ-7 beta-lactamase genes. Antimicrob Agents Chemother. 1992 Sep;36(9):1817-20. [Article]
- Brun T, Peduzzi J, Canica MM, Paul G, Nevot P, Barthelemy M, Labia R: 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 Jul 1;120(1-2):111-7. [Article]
- Jelsch C, Lenfant F, Masson JM, Samama JP: Beta-lactamase TEM1 of E. coli. Crystal structure determination at 2.5 A resolution. FEBS Lett. 1992 Mar 9;299(2):135-42. [Article]
- Jelsch C, Mourey L, Masson JM, Samama JP: Crystal structure of Escherichia coli TEM1 beta-lactamase at 1.8 A resolution. Proteins. 1993 Aug;16(4):364-83. [Article]
- Strynadka NC, Jensen SE, Alzari PM, James MN: 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 Mar;3(3):290-7. [Article]
- Maveyraud L, Pratt RF, Samama JP: Crystal structure of an acylation transition-state analog of the TEM-1 beta-lactamase. Mechanistic implications for class A beta-lactamases. Biochemistry. 1998 Feb 24;37(8):2622-8. [Article]
- Swaren P, Golemi D, Cabantous S, Bulychev A, Maveyraud L, Mobashery S, Samama JP: 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 Jul 27;38(30):9570-6. [Article]
Associated Data
- Drug Relations