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tetR

Gene
tetR
Protein
Tetracycline repressor protein class C
Organism
Escherichia coli
Length
219 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
24.174 kDa
Sequence
MNKLQREAVIRTALELLNDVGMEGLTTRRLAERLGVQQPALYWHFKNKRALLDALAEAMLTINHTHSTPRDDDDWRSFLKGNACSFRRALLAYRDGARIHAGTRPAAPQMEKADAQLRFLCDAGFSAGDATYALMAISYFTVGAVLEQQASEADAEERGEDQLTTSASTMPARLQSAMKIVYEGGPDAAFERGLALIIGGLEKMRLTTNDIEVLKNVDE

Gene
tetR
Protein
Tetracycline repressor protein class D
Organism
Escherichia coli
Length
218 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
24.419 kDa
Sequence
MARLNRESVIDAALELLNETGIDGLTTRKLAQKLGIEQPTLYWHVKNKRALLDALAVEILARHHDYSLPAAGESWQSFLRNNAMSFRRALLRYRDGAKVHLGTRPDEKQYDTVETQLRFMTENGFSLRDGLYAISAVSHFTLGAVLEQQEHTAALTDRPAAPDENLPPLLREALQIMDSDDGEQAFLHGLESLIRGFEVQLTALLQIVGGDKLIIPFC

Gene
tetR
Protein
Tetracycline repressor protein class D
Organism
Salmonella ordonez
Length
218 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
24.419 kDa
Sequence
MARLNRESVIDAALELLNETGIDGLTTRKLAQKLGIEQPTLYWHVKNKRALLDALAVEILARHHDYSLPAAGESWQSFLRNNAMSFRRALLRYRDGAKVHLGTRPDEKQYDTVETQLRFMTENGFSLRDGLYAISAVSHFTLGAVLEQQEHTAALTDRPAAPDENLPPLLREALQIMDSDDGEQAFLHGLESLIRGFEVQLTALLQIVGGDKLIIPFC

Gene
tetR
Protein
Tetracycline repressor protein class H
Organism
Photobacterium damsela subsp. piscicida
Length
218 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
24.419 kDa
Sequence
MARLNRESVIDAALELLNETGIDGLTTRKLAQKLGIEQPTLYWHVKNKRALLDALAVEILARHHDYSLPAAGESWQSFLRNNAMSFRRALLRYRDGAKVHLGTRPDEKQYDTVETQLRFMTENGFSLRDGLYAISAVSHFTLGAVLEQQEHTAALTDRPAAPDENLPPLLREALQIMDSDDGEQAFLHGLESLIRGFEVQLTALLQIVGGDKLIIPFC

Gene
tetR
Protein
Tetracycline repressor protein class A from transposon 1721
Organism
Escherichia coli
Length
216 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
23.32 kDa
Sequence
MTKLQPNTVIRAALDLLNEVGVDGLTTRKLAERLGVQQPALYWHFRNKRALLDALAEAMLAENHTHSVPRADDDWRSFLIGNARSFRQALLAYRDGARIHAGTRPGAPQMETADAQLRFLCEAGFSAGDAVNALMTISYFTVGAVLEEQAGDSDAGERGGTVEQAPLSPLLRAAIDAFDEAGPDAAFEQGLAVIVDGLAKRRLVVRNVEGPRKGDD

Gene
tetR
Protein
Tetracycline repressor protein class E
Organism
Escherichia coli
Length
211 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
23.585 kDa
Sequence
MARLSLDDVISMALTLLDSEGLEGLTTRKLAQSLKIEQPTLYWHVRNKQTLMNMLSEAILAKHHTRSAPLPTESWQQFLQENALSFRKALLVHRDGARLHIGTSPTPPQFEQAEAQLRCLCDAGFSVEEALFILQSISHFTLGAVLEEQATNQIENNHVIDAAPPLLQEAFNIQARTSAEMAFHFGLKSLIFGFSAQLDEKKHTPIEDGNK

Gene
tetR
Protein
Tetracycline repressor protein class G
Organism
Vibrio anguillarum
Length
210 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
23.596 kDa
Sequence
MTKLDKGTVIAAGLELLNEVGMDSLTTRKLAERLKVQQPALYWHFQNKRALLDALPEAMLRERHTRSLPEENEDWRVFLKENALSFRTALLSYRDGARIHAGTRPTEPNFGTAETQIRFLCAEGFCPKRAVWALRAVSHYVVGSVLEQQASDADERVPDRPDVSEQAPSSFLHVLFHELETDGMDAAFNFGLDSLIAGFERLRAAVLATD

Gene
tetR
Protein
Tetracycline repressor protein class H
Organism
Pasteurella multocida
Length
207 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
23.156 kDa
Sequence
MAKLDKEQVIDDALILLNEVGIEGLTTRNVAQKIGVEQPTLYWHVKNKRALLDALAETILQKHHHHVLPLPNETWQDFLRNNAKSFRQALLMYRDGGKIHAGTRPSESQFETSEQQLQFLCDAGFSLSQAVYALSSIAHFTLGSVLETQEHQESQKEREKVETDTVAYPPLLTQAVAIMDSDNGDAAFLFVLDVMISGLETVLKSAK

Gene
tetR
Protein
Tetracycline repressor protein class B from transposon Tn10
Organism
Escherichia coli
Length
207 amino acids
Function
TetR is the repressor of the tetracycline resistance element; its N-terminal region forms a helix-turn-helix structure and binds DNA. Binding of tetracycline to TetR reduces the repressor affinity for the tetracycline resistance gene (tetA) promoter operator sites.
Mass
23.355 kDa
Sequence
MSRLDKSKVINSALELLNEVGIEGLTTRKLAQKLGVEQPTLYWHVKNKRALLDALAIEMLDRHHTHFCPLEGESWQDFLRNNAKSFRCALLSHRDGAKVHLGTRPTEKQYETLENQLAFLCQQGFSLENALYALSAVGHFTLGCVLEDQEHQVAKEERETPTTDSMPPLLRQAIELFDHQGAEPAFLFGLELIICGLEKQLKCESGS