Function

Catalyzes the covalent attachment of the prokaryotic ubiquitin-like protein modifier Pup to the proteasomal substrate proteins, thereby targeting them for proteasomal degradation. This tagging system is termed pupylation. The ligation reaction involves the side-chain carboxylate of the C-terminal glutamate of Pup and the side-chain amino group of a substrate lysine. PafA is required to confer resistance against the lethal effects of reactive nitrogen intermediates (RNI), antimicrobial molecules produced by activated macrophages and other cell types. {ECO:0000269|PubMed:14671303, ECO:0000269|PubMed:17082771, ECO:0000269|PubMed:19448618, ECO:0000269|PubMed:20355727}.

Family

Pup ligase/Pup deamidase family, Pup-conjugating enzyme subfamily

GO

• acid-amino acid ligase activity GO:0016881 molecular_function
• response to nitrosative stress GO:0051409 biological_process
• plasma membrane GO:0005886 cellular_component
• protein pupylation GO:0070490 biological_process
• ATP binding GO:0005524 molecular_function
• cell wall GO:0005618 cellular_component
• ubiquitin-like protein transferase activity GO:0019787 molecular_function
• modification-dependent protein catabolic process GO:0019941 biological_process
• magnesium ion binding GO:0000287 molecular_function
• pathogenesis GO:0009405 biological_process
• cellular response to nitric oxide GO:0071732 biological_process
• proteasomal protein catabolic process GO:0010498 biological_process

InterPro

• IPR022279
• IPR004347

UniProt

P9WNU7

GenBank

Rv2097c

EnsemblBacteria

Rv2097c

Mycobrowser

Rv2097c

Rv2097c doesn't seem to be a targeted by any drug.

Rv2097c doesn't seem to be involved in any pathway.