lnuA, historically named linA in Staphylococcus haemolyticus, encodes a lincosamide resistance enzyme. The enzyme family inactivates lincomycin and clindamycin by O-nucleotidylation/adenylation, producing lincosamide 5'-adenylate derivatives. The fetched GOA file is empty for this accession, and GO lacks a lincosamide O-nucleotidyltransferase molecular-function term.
The preferred accession for this review is P06107. These relationships are manually assessed.
Reviewed 2026-10-19 · Searched: UP000306300
Retain P06107 as the primary Swiss-Prot accession. The reference-proteome search returned no significant hit to this lincosamide-resistance protein at the documented search settings. This does not establish absence from the species or its accessory genome. No alternative accession is asserted.
MMseqs2 searched 2,337 sequences across UP000306300 at E <= 1e-5 and sensitivity 7.5, returning 0 hits. The search table and candidate FASTA are empty; no alignments were generated. The heuristic search does not establish genomic absence or unique locus identity.
file:STAHA/lnuA/lnuA-record-evidence.yaml
target_sequence_count: 2337
file:STAHA/lnuA/lnuA-record-evidence.yaml
candidate_count: 0
The primary accession is outside every searched exact-taxon reference proteome.
file:STAHA/lnuA/lnuA-record-evidence.yaml
primary_in_any_reference_proteome: false
Sampled UniSave observations: 11-NOV-2015, entry version 36.: no Proteomes cross-reference; 02-DEC-2020, entry version 43.: no Proteomes cross-reference; 24-JUL-2024, entry version 50.: no Proteomes cross-reference. These dated observations do not establish uninterrupted membership/absence, the exact change date, or UniProt's motivation.
file:STAHA/lnuA/lnuA-record-evidence.yaml
entry_date: 11-NOV-2015, entry version 36. proteomes: []
file:STAHA/lnuA/lnuA-record-evidence.yaml
entry_date: 02-DEC-2020, entry version 43. proteomes: []
file:STAHA/lnuA/lnuA-record-evidence.yaml
entry_date: 24-JUL-2024, entry version 50. proteomes: []
Definition: Catalysis of the transfer of a nucleotidyl group from a nucleoside 5'-triphosphate donor to a lincosamide antibiotic such as lincomycin or clindamycin, producing an O-nucleotidylated lincosamide with reduced antibiotic activity.
Justification: The Lnu/LinA mechanism is a direct antibiotic-inactivation activity, but GO currently lacks a lincosamide O-nucleotidyltransferase term. The AMR mapping records this as an explicit NoTermFound gap.
Parent term: transferase activity
Mappings:
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0046677 response to antibiotic | RCA file:genes/STAHA/lnuA/lnuA-uniprot.txt | NEW | Summary: NEW high-level process annotation for a lincosamide-resistance determinant. Reason: The GOA TSV is empty, but the UniProt flat file carries response to antibiotic and CARD identifies the entry as lnuA, an antibiotic inactivation determinant. Supporting Evidence: file:genes/STAHA/lnuA/lnuA-uniprot.txt DR CARD; ARO:3002835; lnuA; ARO:0001004; antibiotic inactivation. PMID:3091456 confers resistance to lincomycin by inactivating it in Staphylococcus haemolyticus. |
| GO:0016740 transferase activity | RCA PMID:2846528 Inactivation of lincosaminide antibiotics in Staphylococcus.... | NEW | Summary: NEW broad molecular-function annotation for lincosamide O-nucleotidyltransferase activity. Reason: GO lacks a lincosamide O-nucleotidyltransferase term. The broad transferase parent is a defensible interim MF, but the proposed new term below is the biologically useful target. Supporting Evidence: PMID:2846528 Identification of lincosaminide O-nucleotidyltransferases PMID:2846528 linA encoding the 3-lincomycin, 4-clindamycin O-nucleotidyltransferase |
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Experiment: Reconstitute purified LnuA/LinA with lincomycin and clindamycin plus ATP, GTP, CTP, or UTP donors and quantify nucleotidylated products by NMR or LC-MS.
Type: in vitro enzyme assay
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