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Literature summary for 3.4.24.B17 extracted from

  • Fuehrer, F.; Mueller, A.; Baumann, H.; Langklotz, S.; Kutscher, B.; Narberhaus, F.
    Sequence and length recognition of the C-terminal turnover element of LpxC, a soluble substrate of the membrane-bound FtsH protease (2007), J. Mol. Biol., 372, 485-496.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
membrane
-
Escherichia coli 16020
-

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ dependent Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli W3110 / ATCC 27325
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
protein SecY + H2O
-
Escherichia coli ?
-
?
protein SecY + H2O
-
Escherichia coli W3110 / ATCC 27325 ?
-
?
protein YccA + H2O
-
Escherichia coli ?
-
?
protein YccA + H2O
-
Escherichia coli W3110 / ATCC 27325 ?
-
?
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase + H2O
-
Escherichia coli ?
-
?
UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase + H2O
-
Escherichia coli W3110 / ATCC 27325 ?
-
?
uncomplexed form of the subunit alpha of the proton ATPase F0 + H2O
-
Escherichia coli ?
-
?
uncomplexed form of the subunit alpha of the proton ATPase F0 + H2O
-
Escherichia coli W3110 / ATCC 27325 ?
-
?

Subunits

Subunits Comment Organism
homohexamer the FtsH holoenzyme is a ring-shaped homohexamer forming a complex of up to 1 MDa together with the membrane proteins QmcA and HflKC Escherichia coli

Synonyms

Synonyms Comment Organism
FtsH
-
Escherichia coli