lpqT Resolved · high auto-curated

H37Rv Rv1016c · MTBC0 - · 226 aa · 1134785–1135465 (-) · RefSeq NP_215532.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)lipoprotein LpqT
MTBC0 PGAP re-annotation
Revised (this work)Lipoprotein LpqT. Pfam: Lpp-LpqN (PF10738.16).

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

Annotated on the H37Rv protein: this gene has no 1:1 ancestral MTBC0 anchor (PE/PPE, paralogue, IS element, or otherwise unanchored CDS).

Curated reference (UniProt)

UniProt P9WK59 SwissProt · reviewed · Evidence at protein level
UniProt namePutative lipoprotein LpqT

UniProt still lists this protein as Putative lipoprotein LpqT; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category S Function unknown
Preferred namelpqT
eggNOG descriptionProbable lipoprotein LpqN
Orthologous group2APGE
Gene Ontology (6) GO:0005575, GO:0005618, GO:0005623, GO:0030312, GO:0044464, GO:0071944

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) pseudogene candidate

pN/pS n/a
Polymorphic sites (≥ 0.1% of strains) 0 synonymous, 2 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 10.41% of strains (15110) · clonal

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
Lpp-LpqNPF10738.16 1.2e-6457–224 Probable lipoprotein LpqN

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

Closest characterised functional partner: prsA (ribose-phosphate pyrophosphokinase), high confidence from genomic context alone (score 834 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1017c prsA ribose-phosphate pyrophosphokinase 833 834 ctx neighborhood:832
Rv1018c glmU bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase 748 749 ctx neighborhood:747
Rv1015c rplY 50S ribosomal protein L25/general stress protein Ctc 735 735 ctx neighborhood:732
Rv1014c pth peptidyl-tRNA hydrolase 730 729 ctx neighborhood:728
Rv1019 transcriptional regulator 667 668 ctx neighborhood:667
Rv0418 lpqL lipoprotein aminopeptidase LpqL 414 52 textmining:408
Rv0237 lpqI lipoprotein LpqI 551 51 textmining:547
Rv3044 fecB FeIII-dicitrate-binding periplasmic lipoprotein 529 50 textmining:525
Rv2945c lppX lipoprotein LppX 468 50 textmining:463
Rv3244c lpqB lipoprotein LpqB 700 47 textmining:698
Rv1368 lprF lipoprotein LprF 598 47 textmining:596
Rv2403c lppR lipoprotein LppR 561 47 textmining:559
Rv0419 lpqM lipoprotein peptidase LpqM 543 47 textmining:541
Rv2138 lppL lipoprotein LppL 437 47 textmining:434
Rv3576 lppH lipoprotein LppH 437 47 textmining:434

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

  • Annotation from H37Rv (no MTBC0 1:1 anchor; H37Rv protein used): lipoprotein LpqT
  • Pfam (hmmscan --cut_ga): Lpp-LpqN PF10738.16 (E=1e-64)
  • (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_215532.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Lpp-LpqN (PF10738.16)
  • 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 2APGE
  • Curated reference: UniProt P9WK59 (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 — 21 functional partner(s); context anchor prsA
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv1016c|lpqT
MAGRRCPQDSVRPLAVAVAVATLAMSAVACGPKSPDFQSILSTSPTTSAVSTTTEVPVPLWKYLESVGVTGEPVAPSSLTDLTVSIPTPPGWAPMKNPNITPNTEMIAKGESYPTAMLMVFKLHRDFDIAEALKHGTADARLSTNFTELDSSTADFNGFPSSMIQGSYDLHGRRLHTWNRIVFPTGAPPAKQRYLVQLTITSLANEAVKHASDIEAIIAGFVVAAK