gatC

Summary: gatC performs a defined chemical step supplying translation substrates.

Reason: GatABC covalently amidates an amino acid already esterified to tRNA. The direct process is charged-tRNA amino acid modification, not formation of the amino-acid–tRNA ester bond. This is a lateral mechanistic correction rather than an assertion that GO:0019988 is a descendant of translation.

Proposed replacements: charged-tRNA amino acid modification

Summary: The conserved GatC scaffold helps maintain accurate aminoacyl-tRNA supply.

Reason: GatC stabilizes the GatABC complex that converts mischarged Asp-tRNA(Asn) into the cognate translation substrate. The broad fidelity term includes this control of charged-tRNA identity; it does not require direct regulation of ribosomal decoding. Native Mycobacterium smegmatis GatC perturbation changes mistranslation, and PAO1 transamidosome biochemistry demonstrates protection of the mischarged intermediate. Together with the target HAMAP-supported GatC architecture, these support a conserved role. Neither source measures KT2440 error rates, and the mycobacterial adaptive antibiotic-tolerance phenotype is not transferred.

Summary: GatABC modifies a charged amino acid; the former pathway-variant BP is obsolete.

Reason: Current QuickGO explicitly retires GO:0070681 and distinguishes GatCAB modification of already-charged tRNA from charging itself. KT2440 conserved GatABC and non-discriminating AspS support the Asn-forming modification route by inference. PAO1 shows an additional in vitro Gln-forming capacity with supplied heterologous substrate, not a native KT2440 Gln-transamidation pathway. Replace the obsolete overly specific pathway claim with the supported modification process.

Proposed replacements: charged-tRNA amino acid modification

Summary: gatC is a structural member of the GatABC heterotrimer.

Reason: The exact curated A/B/C heterotrimer assignment supports complex membership. Its historical Gln-oriented name does not exclude the native Asn-forming implementation, and no alternative oligomeric stoichiometry is inferred.

Summary: gatC contributes to Asn formation on tRNA within GatABC.

Reason: GatA supplies glutamine-derived ammonia, GatB carries the tRNA-bound acceptor activation/amidation machinery, and GatC supports the complex. The exact KT2440 conserved family/rule assignments and native PAO1 Asn-transamidation assay support the target capability by homology; no isolated-subunit complete reaction or direct KT2440 kinetics is asserted.