pth Resolved · high auto-curated

H37Rv Rv1014c · MTBC0 mtbc0_001089 · 191 aa · 1140670–1141245 (-) · RefSeq NP_215530.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)peptidyl-tRNA hydrolase
MTBC0 PGAP re-annotationaminoacyl-tRNA hydrolase
Revised (this work)Aminoacyl-tRNA hydrolase. Pfam: Pept_tRNA_hydro (PF01195.26).

Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.

Curated reference (UniProt)

UniProt P9WHN7 SwissProt · reviewed · Evidence at protein level
UniProt namePeptidyl-tRNA hydrolase
EC (curated) EC 3.1.1.29
Curated functionHydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling..; FUNCTION: Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes..; FUNCTION: Important for recycling peptidyl-tRNA(Pro) that has dropped off during the incorporation of proline into a growing peptide. Probably cleaves the acetyl group off acetylated aminoacylated-tRNA (produced by TacT for exam.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category J Translation, ribosomal structure and biogenesis
Preferred namepth
eggNOG descriptionThe natural substrate for this enzyme may be peptidyl- tRNAs which drop off the ribosome during protein synthesis
Orthologous groupCOG0193
EC number EC 3.1.1.29
KEGG orthology K01056
Gene Ontology (16) GO:0003674, GO:0003824, GO:0004045, GO:0005575, GO:0005623, GO:0005886, GO:0008150, GO:0016020, GO:0016787, GO:0016788, GO:0040007, GO:0044464 +4 more

Orthology-based transfer (eggNOG 5.0.2, diamond). EC/KO/GO/CAZy are computed annotations, not manual curation; cross-check against the primary literature before treating a specific reaction as established.

Conservation & selection (intra-MTBC, 145 209 strains)

pN/pS 1.037 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 1 synonymous, 3 missense, 0 nonsense, 0 frameshift

pN/pS from segregating SNPs (singletons removed) normalised by possible sites. Low pN/pS = purifying selection (a strong signal that a "hypothetical" is a real, constrained gene). A high pN/pS is ambiguous: relaxed constraint or positive selection (drug resistance, antigenic variation) inflate it; e.g. rpoB/katG/pncA score high here for resistance, not loss of function. A clonal disruption (one allele over a clade) suggests lineage pseudogenisation; a convergent one (many independent alleles) is typical of resistance loss-of-function.

Domains (Pfam, hmmscan --cut_ga)

PfamAccessioni-EvalueResiduesDescription
Pept_tRNA_hydroPF01195.26 4.8e-676–189 Peptidyl-tRNA hydrolase

Functional interaction network (STRING v12, guilt-by-association)

Closest characterised functional partner: rplY (50S ribosomal protein L25/general stress protein Ctc), high confidence from genomic context alone (score 940 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1015c rplY 50S ribosomal protein L25/general stress protein Ctc 942 940 ctx neighborhood:874 coexpression:486
Rv1112 ychF GTP-binding protein 862 820 coexpression:710
Rv1020 mfd transcription-repair coupling factor 775 742 coexpression:644
Rv1016c lpqT lipoprotein LpqT 730 729 ctx neighborhood:728
Rv3625c mesJ tRNA(Ile)-lysidine synthase 692 673 coexpression:646
Rv1307 atpH ATP synthase subunit b/delta 675 656 coexpression:648
Rv1017c prsA ribose-phosphate pyrophosphokinase 663 648 ctx neighborhood:498
Rv2404c lepA GTP-binding protein LepA 668 627 ctx cooccurence:562
Rv2882c frr ribosome recycling factor 709 621 ctx cooccurence:612
Rv3443c rplM 50S ribosomal protein L13 612 613 ctx cooccurence:515
Rv3105c prfB peptide chain release factor PrfB 693 612 coexpression:493
Rv3456c rplQ 50S ribosomal protein L17 665 607 ctx cooccurence:585
Rv0690c hyp hypothetical protein 574 573 ctx fusion:538
Rv1402 priA primosomal protein N' 535 536 coexpression:512
Rv1299 prfA peptide chain release factor PrfA 833 535 ctx cooccurence:494 textmining:656

STRING combines evidence channels (neighborhood, fusion, cooccurrence, coexpression, experimental, database, text-mining) into a 0–1000 score. The ctx badge marks edges carried by the genomic-context channels (conserved neighborhood, fusion, phylogenetic co-occurrence), which are independent of orthology and structure and the strongest signal for an unknown gene. The no text-mining column recomputes the score from data alone, so a link that does not depend on the literature is visible. Association is a function hypothesis, not proof: corroborate with the operon context and the primary literature before assigning a function.

Evidence

  • Legacy H37Rv annotation: peptidyl-tRNA hydrolase
  • MTBC0 PGAP product: aminoacyl-tRNA hydrolase
  • Pfam (hmmscan --cut_ga): Pept_tRNA_hydro PF01195.26 (E=5e-67)
  • (auto-curated by rules from PGAP + Pfam + Foldseek; not hand-reviewed)

Sources

  • Ancestral sequence & coordinates: Harrison LB et al. (2024), An imputed ancestral reference genome for the MTBC, doi:10.1101/2023.09.07.556366
  • Product annotation: NCBI PGAP on MTBC0; legacy from H37Rv NC_000962.3 (RefSeq NP_215530.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Pept_tRNA_hydro (PF01195.26)
  • Sequence-level signal: ESM Atlas (EvolutionaryScale × BioHub) — exploratory
  • Controlled vocabulary: eggNOG-mapper 2.1.12 (Cantalapiedra et al. 2021, doi:10.1093/molbev/msab293), eggNOG 5.0 DB (Huerta-Cepas et al. 2019) — OG COG0193
  • Curated reference: UniProt P9WHN7 (SwissProt, reviewed; Evidence at protein level)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 101 functional partner(s); context anchor rplY
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001089|Rv1014c|pth
MAEPLLVVGLGNPGANYARTRHNLGFVVADLLAARLGAKFKAHKRSGAEVATGRSAGRSLVLAKPRCYMNESGRQIGPLAKFYSVAPANIIVIHDDLDLEFGRIRLKIGGGEGGHNGLRSVVAALGTKDFQRVRIGIGRPPGRKDPAAFVLENFTPAERAEVPTICEQAADATELLIEQGMEPAQNRVHAW