Beta-lactamase TEM

Details

Name
Beta-lactamase TEM
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
Organism
Escherichia coli
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
Functions
beta-lactamase activity
Processes
beta-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
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
ResourceLink
UniProtKB IDP62593
UniProtKB Entry NameBLAT_ECOLX
GenBank Protein ID208959
GenBank Gene IDJ01749
General References
  1. 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]
  2. Sutcliffe JG: Complete nucleotide sequence of the Escherichia coli plasmid pBR322. Cold Spring Harb Symp Quant Biol. 1979;43 Pt 1:77-90. [Article]
  3. 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]
  4. 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]
  5. 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]
  6. 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]
  7. 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]
  8. 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]
  9. 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]
  10. 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]
  11. 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]
  12. 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]
  13. 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]
  14. 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]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB074641(R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACIDexperimentalunknownDetails
DB026141(R)-1-Acetamido-2-(3-Carboxyphenyl)Ethyl Boronic AcidexperimentalunknownDetails
DB07466(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACIDexperimentalunknownDetails
DB04035Ceftazidime BATSIexperimentalunknownDetails
DB04037N,N-Bis(4-Chlorobenzyl)-1h-1,2,3,4-Tetraazol-5-AmineexperimentalunknownDetails
DB07599[(2-AMINO-ALPHA-METHOXYIMINO-4-THIAZOLYLACETYL)AMINO]METHYLBORONIC ACIDexperimentalunknownDetails
DB02642[[N-(Benzyloxycarbonyl)Amino]Methyl]PhosphateexperimentalunknownDetails
DB044303-(4-Phenylamino-Phenylamino)-2-(1h-Tetrazol-5-Yl)-AcrylonitrileexperimentalunknownDetails
DB02841[(2-Ethoxy-1-Naphthoyl)Amino]Methylboronic AcidexperimentalunknownDetails
DB085513-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acidexperimentalunknownDetails
DB09060AvibactamapprovedyesinhibitorDetails
DB12107Vaborbactamapproved, investigationalyesinhibitorDetails
DB12377Relebactamapproved, investigationalyesinhibitorDetails
DB01598ImipenemapprovednosubstrateDetails
DB01053Benzylpenicillinapproved, vet_approvedunknownsubstrateDetails