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Literature summary for 7.4.2.8 extracted from

  • Py, B.; Loiseau, L.; Barras, F.
    Assembly of the type II secretion machinery of Erwinia chrysanthemi: direct interaction and associated conformational change between OutE, the putative ATP-binding component and the membrane protein OutL (1999), J. Mol. Biol., 289, 659-670.
    View publication on PubMed

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O Dickeya chrysanthemi type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases ADP + phosphate
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Organism

Organism UniProt Comment Textmining
Dickeya chrysanthemi
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type II protein secretion system
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O
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Dickeya chrysanthemi ADP + phosphate
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?
ATP + H2O type II enzyme system: secretion of a large number of enzymes, including cellulases and pectinases Dickeya chrysanthemi ADP + phosphate
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?

Subunits

Subunits Comment Organism
More the Out proteins form a membrane-associated multiprotein complex, OutE is the putative ATP binding component and OutL is an inner membrane protein. OutE and OutL interact directly. OutE induces a conformational change in OutL, in both its cytoplasmic and periplasmic domains. The secretion process requires a conformational change in OutE which depends on both the interaction with OutL and on the presence of an intact Walker A motif in OutE Dickeya chrysanthemi