lipJ Family assigned · medium auto-curated

H37Rv Rv1900c · MTBC0 mtbc0_002015 · 462 aa · 2164355–2165743 (-) · RefSeq NP_216416.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)lignin peroxidase LipJ
MTBC0 PGAP re-annotationadenylate/guanylate cyclase domain-containing protein
Revised (this work)Adenylate/guanylate cyclase domain-containing protein. Pfam: Abhydrolase_1 (PF00561.27), Guanylate_cyc (PF00211.26).

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

Curated reference (UniProt)

UniProt O07732 SwissProt · reviewed · Evidence at protein level
UniProt nameBifunctional lipase/adenylate cyclase LipJ [Includes: Lipase
EC (curated) EC 3.1.1.-, EC 4.6.1.1
Curated functionMay play a role in cell wall modulation. The N-terminal domain exhibits lipolytic activity. In vitro, hydrolyzes various p-nitrophenyl (pNP) esters. pNP-decanoate (C10) is the best substrate, followed by pNP-octonate (C8), pNP-laurate (C12) and pNP-butyrate (C4). Exhibits lower activity with pNP-acetate (C2), pNP-myristate (C14) and pNP-palmitate (C16). Can also use tributyrin. The C-terminal domain catalyzes the biosynthesis of cyclic AMP (cAMP) from ATP. It has a guanylyl cyclase side-activity, corresponding to 7% of the adenylate cyclase activity.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category I Lipid transport and metabolism
T Signal transduction mechanisms
Preferred namelipJ
eggNOG descriptionPFAM Adenylate and Guanylate cyclase catalytic domain
Orthologous groupCOG2114

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 1.747 · diversifying/relaxed
Polymorphic sites (≥ 0.1% of strains) 2 synonymous, 10 missense, 0 nonsense, 1 frameshift
Disruption 1 distinct premature-stop/frameshift site(s); most common in 0.50% of strains (727) · 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
Abhydrolase_1PF00561.27 2.5e-0863–158 alpha/beta hydrolase fold
Guanylate_cycPF00211.26 1.2e-11296–445 Adenylate and Guanylate cyclase catalytic domain

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

Closest characterised functional partner: lppD (lipoprotein LppD), high confidence from genomic context alone (score 788 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv1899c lppD lipoprotein LppD 789 788 ctx neighborhood:780
Rv1901 cinA competence damage-inducible protein CinA 692 693 ctx neighborhood:686
Rv1363c membrane protein 646 633
Rv1359 transcriptional regulator 603 603 ctx cooccurence:603
Rv2048c pks12 polyketide synthase 637 593 experimental:455
Rv0199 membrane protein 601 586
Rv3492c Mce associated protein 600 584
Rv0200 transmembrane protein 600 584
Rv0178 Mce associated membrane protein 598 583
Rv1972 Mce associated membrane protein 598 582
Rv2390c hyp hypothetical protein 597 582
Rv1362c membrane protein 597 582
Rv1973 Mce associated membrane protein 597 582
Rv0177 Mce associated protein 597 582
Rv1902c nanT sialic acid-transport integral membrane protein NanT 545 545 ctx neighborhood:541

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: lignin peroxidase LipJ
  • MTBC0 PGAP product: adenylate/guanylate cyclase domain-containing protein
  • Pfam (hmmscan --cut_ga): Abhydrolase_1 PF00561.27 (E=2e-08), Guanylate_cyc PF00211.26 (E=1e-11)
  • (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_216416.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Abhydrolase_1 (PF00561.27), Guanylate_cyc (PF00211.26)
  • 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 COG2114
  • Curated reference: UniProt O07732 (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 — 61 functional partner(s); context anchor lppD
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002015|Rv1900c|lipJ
MAQAPHIHRTRYAKCGDMDIAYQVLGDGPTDLLVLPGPFVPIDSIDDEPSLYRFHRRLASFSRVIRLDHRGVGLSSRLAAITTLGPKFWAQDAIAVMDAVGCEQATIFAPSFHAMNGLVLAADYPERVRSLIVVNGSARPLWAPDYPVGAQVRRADPFLTVALEPDAVERGFDVLSIVAPTVAGDDVFRAWWDLAGNRAGPPSMARAVSKVIAEADVRDVLGHIEAPTLILHRVGSTYIPVGHGRYLAEHIAGSRLVELPGTDTLYWVGDTGPMLDEIEEFITGVRGGADAERMLATIMFTDIVGSTQHAAALGDDRWRDLLDNHDTIVCHEIQRFGGREVNTAGDGFVATFTSPSAAIACADDIVDAVAALGIEVRIGIHAGEVEVRDASHGTDVAGVAVHIGARVCALAGPSEVLVSSTVRDIVAGSRHRFAERGEQELKGVPGRWRLCVLMRDDATRTR