BIRA

Contains an N-terminal helix-turn-helix DNA-binding domain, connected via a linker to the central catalytic domain and the C-terminal domain, which plays roles in dimerization, catalytic function and DNA binding. The N-terminal domain is required for both ligase and repressor activities. It may orient the active site and thereby play an important role in enzymatic activity.

Acts both as a biotin--[acetyl-CoA-carboxylase] ligase and a biotin-operon repressor. In the presence of ATP, BirA activates biotin to form the BirA-biotinyl-5'-adenylate (BirA-bio-5'-AMP or holoBirA) complex. HoloBirA can either transfer the biotinyl moiety to the biotin carboxyl carrier protein (BCCP) subunit of acetyl-CoA carboxylase, or bind to the biotin operator site and inhibit transcription of the operon.

Belongs to the biotin--protein ligase family.

bioR, dhbB, b3973, JW3941, birA, Bifunctional ligase/repressor BirA, Biotin operon repressor, Biotin--[acetyl-CoA-carboxylase] ligase, Biotin--protein ligase, Biotin-[acetyl-CoA carboxylase] synthetase

• swissprot:P06709

Proteins

35312Da