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Strain identifier

BacDive ID: 16714

Type strain: Yes

Species: Thermus aquaticus

Strain Designation: YT-1

Culture col. no.: DSM 625, ATCC 25104, JCM 10724, LMG 8924, NBRC 103206, NCIMB 11243

Strain history: DSM 625 <-- T. D. Brock YT-1.

NCBI tax ID(s): 271 (species)

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Thermus aquaticus YT-1 is a thermophilic bacterium that was isolated from hot spring.

  1. thermophilic
  2. 16S sequence
  3. Bacteria
  4. genome sequence
  • Availability in culture collections External linksarrow_down
  • [Ref.: #328] Culture collection no. DSM 625, ATCC 25104, JCM 10724, LMG 8924, NBRC 103206, NCIMB 11243
    [Ref.: #20218] Associated Passport(s) in StrainInfo 22176, 22173
    Literature: Only first 10 entries are displayed. Click here to see all.Click here to see only first 10 entries.
    Topicarrow to sort Titlearrow to sort Authorsarrow to sort Journalarrow to sort DOIarrow to sort Yeararrow to sort
    Enzymology Molecular cloning, expression, purification, and characterization of fructose-1,6-bisphosphate aldolase from Thermus aquaticus. Sauve V, Sygusch J Protein Expr Purif 10.1006/prep.2000.1380 2001 *
    Enzymology Crystallization and preliminary crystallographic analysis of an NADH oxidase that functions in peroxide reduction in Thermus aquaticus YT-1. Mac Sweeney A, D'Arcy A, Higgins TM, Mayhew SG, Toomey D, Walsh MA Acta Crystallogr D Biol Crystallogr 10.1107/S090744499800941X 1999 *
    Enzymology Purification and characterisation of NADH oxidase from Thermus aquaticus YT-1 and evidence that it functions in a peroxide-reduction system. Toomey D, Mayhew SG Eur J Biochem 10.1046/j.1432-1327.1998.2510935.x 1998 *
    Enzymology Cloning of genes of the aminopeptidase T family from Thermus thermophilus HB8 and Bacillus stearothermophilus NCIB8924: apparent similarity to the leucyl aminopeptidase family. Motoshima H, Minagawa E, Tsukasaki F, Kaminogawa S Biosci Biotechnol Biochem 10.1271/bbb.61.1710 1997 *
    Enzymology Cloning and analysis of the DNA polymerase-encoding gene from Thermus caldophilus GK24. Kwon ST, Kim JS, Park JH, Kim HK, Lee DS Mol Cells 1997 *
    Enzymology Molecular cloning and nucleotide sequence of the aminopeptidase T gene of Thermus aquaticus YT-1 and its high-level expression in Escherichia coli. Motoshima H, Azuma N, Kaminogawa S, Ono M, Minagawa E, Matsuzawa H, Ohta T, Yamauchi K Agric Biol Chem 1990 *
    Enzymology Enhancement of the thermostability of subtilisin E by introduction of a disulfide bond engineered on the basis of structural comparison with a thermophilic serine protease. Takagi H, Takahashi T, Momose H, Inouye M, Maeda Y, Matsuzawa H, Ohta T J Biol Chem S0021-9258(19)39230-0 1990 *
    Enzymology NADH oxidase from the extreme thermophile Thermus aquaticus YT-1. Purification and characterisation. Cocco D, Rinaldi A, Savini I, Cooper JM, Bannister JV Eur J Biochem 10.1111/j.1432-1033.1988.tb14093.x 1988 *
    Metabolism The third restriction-modification system from Thermus aquaticus YT-1: solving the riddle of two TaqII specificities. Skowron PM, Anton BP, Czajkowska E, Zebrowska J, Sulecka E, Krefft D, Jezewska-Frackowiak J, Zolnierkiewicz O, Witkowska M, Morgan RD, Wilson GG, Fomenkov A, Roberts RJ, Zylicz-Stachula A Nucleic Acids Res 10.1093/nar/gkx599 2017 *
    Enzymology Highly conserved salt bridge stabilizes a proteinase K subfamily enzyme, Aqualysin I, from Thermus aquaticus YT-1. Sakaguchi M, Osaku K, Maejima S, Ohno N, Sugahara Y, Oyama F, Kawakita M AMB Express 10.1186/s13568-014-0059-2 2014 *

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