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Literature summary 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)

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

Organism

EC Number Organism UniProt Comment Textmining
7.4.2.6 Borreliella burgdorferi H7C7K8 OppA4
-
7.4.2.6 Borreliella burgdorferi B31 H7C7K8 OppA4
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.4.2.6 ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
-
 Borreliella burgdorferi ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
 ?
7.4.2.6 ATP + H2O + oligopeptide-[oligopeptide-binding protein][side 1]
-
 Borreliella burgdorferi B31 ADP + phosphate + oligopeptide[side 2] + [oligopeptide-binding protein][side 1]
-
 ?
7.4.2.6 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]
-
 ?
7.4.2.6 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

EC Number Synonyms Comment Organism
7.4.2.6 oligopeptide transporter
-
 Borreliella burgdorferi
7.4.2.6 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

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