ltp1 Resolved · high auto-curated

H37Rv Rv2790c · MTBC0 mtbc0_002969 · 401 aa · 3121379–3122584 (-) · RefSeq NP_217306.3

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)lipid-transfer protein
MTBC0 PGAP re-annotationlipid-transfer protein
Revised (this work)Lipid-transfer protein. Pfam: Thiolase_N (PF00108.30), Thiolase_C_1 (PF22691.3), Thiolase_C (PF02803.25).

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

Curated reference (UniProt)

UniProt O33332 TrEMBL · unreviewed · Evidence at protein level
UniProt namepropanoyl-CoA C-acyltransferase
EC (curated) EC 2.3.1.176

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
Preferred nameltp1
eggNOG descriptionBelongs to the thiolase family
Orthologous groupCOG0183
EC number EC 2.3.1.16
KEGG orthology K00632
KEGG pathways map00071, map00280, map00281, map00362, map00592, map00642, map01100, map01110, map01120, map01130, map01212
KEGG modules M00087, M00113
Gene Ontology (71) GO:0003674, GO:0003676, GO:0003723, GO:0003729, GO:0003824, GO:0003988, GO:0005488, GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005739 +59 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 0.053 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 12 synonymous, 2 missense, 0 nonsense, 7 frameshift
Disruption 7 distinct premature-stop/frameshift site(s); most common in 0.87% of strains (1270) · convergent

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
Thiolase_NPF00108.30 3.0e-2210–234 Thiolase, N-terminal domain
Thiolase_C_1PF22691.3 7.4e-33269–391 Thiolase C-terminal domain-like
Thiolase_CPF02803.25 4.3e-09275–373 Thiolase, C-terminal domain

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

Closest characterised functional partner: fadE21 (acyl-CoA dehydrogenase FadE21), high confidence from genomic context alone (score 977 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0860 fadB fatty oxidation protein FadB 996 996 coexpression:696 experimental:804 database:942
Rv2789c fadE21 acyl-CoA dehydrogenase FadE21 977 977 ctx neighborhood:847 coexpression:839
Rv0231 fadE4 acyl-CoA dehydrogenase FadE4 953 951 database:900
Rv3140 fadE23 acyl-CoA dehydrogenase FadE23 945 942 database:900
Rv0400c fadE7 acyl-CoA dehydrogenase FadE7 943 942 database:900
Rv0154c fadE2 acyl-CoA dehydrogenase FadE2 943 942 database:900
Rv0975c fadE13 acyl-CoA dehydrogenase FadE13 943 941 database:900
Rv0131c fadE1 acyl-CoA dehydrogenase FadE1 943 941 database:900
Rv3280 accD5 propionyl-CoA carboxylase subunit beta 931 928 database:900
Rv2247 accD6 acetyl-/propionyl-CoA carboxylase subunit beta 930 927 database:900
Rv3523 ltp3 lipid carrier protein 929 927 database:900
Rv0914c lipid carrier protein or keto acyl-CoA thiolase 926 927 database:900
Rv2501c accA1 acetyl/propionyl-CoA carboxylase subuit alpha 928 925 database:900
Rv0973c accA2 acetyl/propionyl-CoA carboxylase subuit alpha 928 925 database:900
Rv3285 accA3 bifunctional protein acetyl-/propionyl-CoA carboxylase subunit alpha AccA 928 925 database:900

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: lipid-transfer protein
  • MTBC0 PGAP product: lipid-transfer protein
  • Pfam (hmmscan --cut_ga): Thiolase_N PF00108.30 (E=3e-22), Thiolase_C_1 PF22691.3 (E=7e-33), Thiolase_C PF02803.25 (E=4e-09)
  • (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_217306.3)
  • Domains: Pfam-A via hmmscan --cut_ga — Thiolase_N (PF00108.30), Thiolase_C_1 (PF22691.3), Thiolase_C (PF02803.25)
  • 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 COG0183
  • Curated reference: UniProt O33332 (TrEMBL, unreviewed; 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 — 153 functional partner(s); context anchor fadE21
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002969|Rv2790c|ltp1
MPNQGSSNKVYVIGVGMTKFEKPGRREGWDYPDMARESGTKALRDAGIDYREVEQGYVGYVYGESTSGQRALYELGMTGIPIVNVNNNCSTGSTALYLGAQAIRGGLADCVLALGFEKMQPGALGGGADDRESPLGRHVKALAEIDEFGFPVAPWMFGAAGREHMKKYGTTAEHFAKIGYKNHKHSVNNPYAQFQDEYTLDDILASKMISDPLTKLQCSPTSDGSAAVVLASEDYLANHNLAGRAVEIVGQAMTTDFASTFDGSARNIIGYDMTVQAAQRVYQQSGLGPKDFGVIELHDCFSANELLLYEALGLCGPGEAPELIDDNQTTYGGRWVVNPSGGLISKGHPLGATGLAQCAELTWQLRGTAEARQVDNVTAALQHNIGLGGAAVVTAYQRAER