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tehB

Gene
tehB
Protein
Probable S-adenosyl-L-methionine-dependent methyltransferase TehB
Organism
Haemophilus influenzae (strain 10810)
Length
286 amino acids
Function
Probable S-adenosyl-L-methionine-dependent methyltransferase. Plays a role in both resistance to oxidative damage and heme uptake/utilization, and is important for virulence of this organism in an animal model of invasive disease. Also protects H.influenzae from tellurite exposure in vitro; however, since H.influenzae grows only in humans, it is unlikely to encounter tellurite in its natural environment, and it is thus probable that tellurite resistance does not represent a biologically relevant role of TehB.
Similarity
Belongs to the TehB family.
Mass
33.05 kDa
Sequence
MKNELICYKQMPVWTKDKLPQMFQEKHNTKVGTWGKLTVLKGKIKFYELTENGDVVAEHIFTPESHIPFVEPQAWHRVEALSDDLECTLGFYCKKEDYFSKKYNMTAIHGDVVDAAKIISPCKVLDLGCGQGRNSLYLSLLGYDVTSWDHNENSIAFLNETKEKENLNISTALYDINAANIQENYDFIVSTVVFMFLNRERVPSIIKNMQEHTNVGGYNLIVAAMSTDDVPCPLPFSFTFAENELKEYYKDWEFLEYNENMGELHKTDENGNRIKMKFATMLARKK

Gene
tehB
Protein
Probable S-adenosyl-L-methionine-dependent methyltransferase TehB
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
286 amino acids
Function
Probable S-adenosyl-L-methionine-dependent methyltransferase. Plays a role in both resistance to oxidative damage and heme uptake/utilization. Also protects H.influenzae from tellurite exposure in vitro; however, since H.influenzae grows only in humans, it is unlikely to encounter tellurite in its natural environment, and it is thus probable that tellurite resistance does not represent a biologically relevant role of TehB (By similarity).
Similarity
Belongs to the TehB family.
Mass
33.02 kDa
Sequence
MKNELICYKQMPVWTKDNLPQMFQEKHNTKVGTWGKLTVLKGKLKFYELTENGDVIAEHIFTPESHIPFVEPQAWHRVEALSDDLECTLGFYCKKEDYFSKKYNTTAIHGDVVDAAKIISPCKVLDLGCGQGRNSLYLSLLGYDVTSWDHNENSIAFLNETKEKENLNISTALYDINAANIQENYDFIVSTVVFMFLNRERVPSIIKNMKEHTNVGGYNLIVAAMSTDDVPCPLPFSFTFAENELKEYYKDWEFLEYNENMGELHKTDENGNRIKMKFATMLARKK

Gene
tehB
Protein
Tellurite methyltransferase
Organism
Escherichia coli (strain K12)
Length
197 amino acids
Function
S-adenosyl-L-methionine dependent methyltransferase that catalyzes the methylation of tellurite and is responsible for tellurite resistance when present in high copy number. Can also methylate selenite and selenium dioxide. Is thus able to detoxify different chalcogens. Cannot methylate arsenic compounds.
Similarity
Belongs to the TehB family.
Mass
22.531 kDa
Sequence
MIIRDENYFTDKYELTRTHSEVLEAVKVVKPGKTLDLGCGNGRNSLYLAANGYDVDAWDKNAMSIANVERIKSIENLDNLHTRVVDLNNLTFDRQYDFILSTVVLMFLEAKTIPGLIANMQRCTKPGGYNLIVAAMDTADYPCTVGFPFAFKEGELRRYYEGWERVKYNEDVGELHRTDANGNRIKLRFATMLARKK