ProS is a class II prolyl-tRNA synthetase that charges tRNA(Pro) and removes alanine errors through pretransfer Ala-AMP hydrolysis and posttransfer Ala-tRNA(Pro) editing. It acts in the cytoplasm of Pseudomonas putida KT2440, using ATP to form the aminoacyl-tRNA substrate for protein synthesis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000166 nucleotide binding | IEA GO_REF:0000002 | MODIFY | Summary: ATP is the nucleotide used to activate proline by proS. Reason: The MF_01569 reaction consumes ATP during formation of the aminoacyl adenylate and releases AMP plus diphosphate. Refine generic nucleotide binding to its supported ATP-binding descendant, without implying that all nucleotides bind equally. Proposed replacements: ATP binding Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0002161 aminoacyl-tRNA deacylase activity | IEA GO_REF:0000120 | MODIFY | Summary: ProS is a class II prolyl-tRNA synthetase that charges tRNA(Pro) and removes alanine errors through pretransfer Ala-AMP hydrolysis and posttransfer Ala-tRNA(Pro) editing. Reason: The source specifically assigns deacylation of Ala-tRNA(Pro), so the supported descendant GO:0043906 is preferable to the generic deacylase term. The Ala-AMP pretransfer reaction is separate, and Cys-tRNA(Pro) editing is explicitly excluded by the curated family rule. HAMAP MF_01569 and the ProRS-INS editing-domain assignment support alanine proofreading. The curated rule explicitly distinguishes mischarged Cys-tRNA(Pro), which is not edited by this ProRS activity. Proposed replacements: Ala-tRNA(Pro) deacylase activity Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt 'posttransfer' editing and involves deacylation of mischarged Ala- file:PSEPK/proS/proS-uniprot.txt tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. |
| GO:0004812 aminoacyl-tRNA ligase activity | IEA GO_REF:0000002 | MODIFY | Summary: The broad ligase annotation can specify proline and tRNA(Pro). Reason: HAMAP MF_01569 and the ProRS-INS editing-domain assignment support alanine proofreading. The curated rule explicitly distinguishes mischarged Cys-tRNA(Pro), which is not edited by this ProRS activity. GO:0004827 is the supported amino-acid-specific descendant of GO:0004812; the parent is biologically correct, not over-annotation. Proposed replacements: proline-tRNA ligase activity Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0004827 proline-tRNA ligase activity | IEA GO_REF:0000120 | ACCEPT | Summary: proS supplies proline-charged tRNA(Pro) through ATP-dependent aminoacylation. Reason: HAMAP MF_01569 and the ProRS-INS editing-domain assignment support alanine proofreading. The curated rule explicitly distinguishes mischarged Cys-tRNA(Pro), which is not edited by this ProRS activity. The independently curated MF_01569 reaction supports this specific MF; electronic provenance does not make a central catalytic function peripheral. Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding is integral to proS-catalysed proline activation. Reason: The curated MF_01569 reaction specifically consumes ATP, and the target retains the corresponding synthetase architecture. This is an essential biochemical property of the charging activity, even though direct KT2440 binding constants have not been measured in the retrieved sources. Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MODIFY | Summary: proS is assigned to the bacterial cytoplasm for translational tRNA charging. Reason: The MF_01569 subcellular-location statement supports this native compartment as a conserved functional inference. The independently retained cytosol assignment gives a more precise compartment within the cytoplasm; this is not a direct KT2440 imaging claim. Proposed replacements: cytosol Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005829 cytosol | IEA GO_REF:0000118 | ACCEPT | Summary: The soluble cytosolic charging pool is the supported location for proS. Reason: The TreeGrafter location inference is coherent with the independently curated MF_01569 cytoplasmic assignment and the enzyme's delivery of aminoacyl-tRNA to bacterial translation. Retain the conserved localization judgment without presenting it as a fractionation assay or inferring exclusion from every other compartment. Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0006418 tRNA aminoacylation for protein translation | IEA GO_REF:0000002 | ACCEPT | Summary: proS catalyses the charging step that supplies proline to ribosomal protein synthesis. Reason: The MF_01569 reaction directly performs aminoacylation, rather than merely affecting translation through a downstream phenotype. Live QuickGO verifies GO:0006418 as current; the old amino-acid-specific biological-process term is obsolete and is not a reason to mark this correct process as over-annotated. Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0006433 prolyl-tRNA aminoacylation | IEA GO_REF:0000120 | MODIFY | Summary: The proline-specific charging chemistry remains supported, but this biological-process ID is obsolete. Reason: The live QuickGO snapshot verifies GO:0006433 as obsolete. Preserve the original machine-sourced ID and label and represent the biological process with current GO:0006418; retain proline specificity in GO:0004827. This is ontology maintenance, not a rejection of the MF_01569 reaction. Proposed replacements: tRNA aminoacylation for protein translation Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt Reaction=tRNA(Pro) + L-proline + ATP = L-prolyl-tRNA(Pro) + AMP + |
| GO:0106074 aminoacyl-tRNA metabolism involved in translational fidelity | IEA GO_REF:0000108 | ACCEPT | Summary: proS proofreading protects aminoacyl-tRNA fidelity. Reason: The source specifically assigns deacylation of Ala-tRNA(Pro), so the supported descendant GO:0043906 is preferable to the generic deacylase term. The Ala-AMP pretransfer reaction is separate, and Cys-tRNA(Pro) editing is explicitly excluded by the curated family rule. Cleavage of the incorrect charged product is direct biochemical participation in fidelity, not merely an inferred growth requirement. Supporting Evidence: file:PSEPK/proS/proS-uniprot.txt 'posttransfer' editing and involves deacylation of mischarged Ala- file:PSEPK/proS/proS-uniprot.txt tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS. |
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