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
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
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
ResourceLink
UniProtKB IDP62593
UniProtKB Entry NameBLAT_ECOLX
GenBank Protein ID208959
GenBank Gene IDJ01749
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 IDag:AAB59737
NCBI Gene ID10076131
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]

Associated Data

Drug Relations
DrugDrug groupPharmacological action?TypeActionsDetails
1(R)-1-ACETAMIDO-2-(3-CARBOXY-2-HYDROXYPHENYL)ETHYL BORONIC ACIDexperimentalunknowntargetDetails
1(R)-1-Acetamido-2-(3-Carboxyphenyl)Ethyl Boronic AcidexperimentalunknowntargetDetails
(1R)-2-PHENYLACETAMIDO-2-(3-CARBOXYPHENYL)ETHYL BORONIC ACIDexperimentalunknowntargetDetails
Ceftazidime BATSIexperimentalunknowntargetDetails
N,N-Bis(4-Chlorobenzyl)-1h-1,2,3,4-Tetraazol-5-AmineexperimentalunknowntargetDetails
[(2-AMINO-ALPHA-METHOXYIMINO-4-THIAZOLYLACETYL)AMINO]METHYLBORONIC ACIDexperimentalunknowntargetDetails
[[N-(Benzyloxycarbonyl)Amino]Methyl]PhosphateexperimentalunknowntargetDetails
3-(4-Phenylamino-Phenylamino)-2-(1h-Tetrazol-5-Yl)-AcrylonitrileexperimentalunknowntargetDetails
[(2-Ethoxy-1-Naphthoyl)Amino]Methylboronic AcidexperimentalunknowntargetDetails
3-{(R)-(Dihydroxyboryl)[(2-thienylacetyl)amino]methyl}benzoic acidexperimentalunknowntargetDetails
AvibactamapprovedyestargetinhibitorDetails
Vaborbactamapproved, investigationalyestargetinhibitorDetails
Relebactamapproved, investigationalyestargetinhibitorDetails
ImipenemapprovednoenzymesubstrateDetails
Benzylpenicillinapproved, vet_approvedunknownenzymesubstrateDetails