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Literature summary for 7.4.2.6 extracted from

  • Groshong, A.M.; Dey, A.; Bezsonova, I.; Caimano, M.J.; Radolf, J.D.
    Peptide uptake is essential for Borrelia burgdorferi viability and involves structural and regulatory complexity of its oligopeptide transporter (2017), mBio, 8, e02047-17 .
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1] Borreliella burgdorferi
-
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1] Borreliella burgdorferi B31
-
ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
?

Organism

Organism UniProt Comment Textmining
Borreliella burgdorferi H7C7K8 OppA4
-
Borreliella burgdorferi B31 H7C7K8 OppA4
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
-
Borreliella burgdorferi ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
?
ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
-
Borreliella burgdorferi B31 ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
?
ATP + H2O + X-Ala-Ala-Ala-[X-Ala-Ala-Ala-binding protein][side 1]
-
Borreliella burgdorferi ADP + phosphate + X-Ala-Ala-Ala[side 2] + [X-Ala-Ala-Ala-binding protein][side 1]
-
?
ATP + H2O + X-Ala-Ala-Ala-[X-Ala-Ala-Ala-binding protein][side 1]
-
Borreliella burgdorferi B31 ADP + phosphate + X-Ala-Ala-Ala[side 2] + [X-Ala-Ala-Ala-binding protein][side 1]
-
?

Synonyms

Synonyms Comment Organism
oligopeptide transporter
-
Borreliella burgdorferi
Opp the Opp system consists of five oligopeptide-binding proteins (OppA1 to OppA5), two heterodimeric cytoplasmic membrane permeases (OppB1C1 and OppB2C2), and a nucleotide-binding domain heterodimer (OppDF) that drives transport by hydrolyzing ATP Borreliella burgdorferi

General Information

General Information Comment Organism
malfunction loss of enzyme function abrogates spirochete growth in vitro Borreliella burgdorferi
physiological function the enzyme is essential for viability, morphogenesis, and virulence within the mammalian host Borreliella burgdorferi