mbtF Resolved · high auto-curated

H37Rv Rv2379c · MTBC0 - · 1461 aa · 2657700–2662085 (-) · RefSeq NP_216895.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)peptide synthetase
MTBC0 PGAP re-annotation
Revised (this work)Peptide synthetase. Pfam: Condensation (PF00668.26), AMP-binding (PF00501.35), AMP-binding_C (PF13193.13), PP-binding (PF00550.32).

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 O05819 TrEMBL · unreviewed · Evidence at protein level
UniProt namePeptide synthetase MbtF

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category Q Secondary metabolites biosynthesis, transport and catabolism
Preferred namembtF
eggNOG descriptionPeptide synthetase
Orthologous groupCOG1020
KEGG orthology K04780, K04792
KEGG pathways map01053

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 0.369 · purifying
Polymorphic sites (≥ 0.1% of strains) 8 synonymous, 8 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
CondensationPF00668.26 1.2e-5917–455 Condensation domain
AMP-bindingPF00501.35 4.9e-69477–813 AMP-binding enzyme
AMP-binding_CPF13193.13 9.1e-08870–943 AMP-binding enzyme C-terminal domain
PP-bindingPF00550.32 3.9e-09970–1031 Phosphopantetheine attachment site

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

Closest characterised functional partner: mbtE (peptide synthetase), high confidence from genomic context alone (score 990 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2377c mbtH hyp hypothetical protein 999 997 ctx neighborhood:834 cooccurence:763 coexpression:867 experimental:564 textmining:847
Rv2380c mbtE peptide synthetase 993 990 ctx neighborhood:799 coexpression:914
Rv2382c mbtC polyketide synthetase 997 986 ctx neighborhood:721 fusion:465 cooccurence:454 coexpression:810 textmining:816
Rv2378c mbtG L-lysine N6-monooxygenase 997 986 ctx neighborhood:881 coexpression:868 textmining:820
Rv2383c mbtB phenyloxazoline synthase 990 982 ctx neighborhood:721 coexpression:910 textmining:515
Rv2381c mbtD polyketide synthetase 994 970 ctx neighborhood:495 cooccurence:548 coexpression:845 textmining:814
Rv2940c mas multifunctional mycocerosic acid synthase 933 922 ctx cooccurence:451 coexpression:466 experimental:721
Rv3825c pks2 phthioceranic/hydroxyphthioceranic acid synthase 933 922 ctx cooccurence:449 coexpression:469 experimental:721
Rv1527c pks5 polyketide synthase 932 922 ctx cooccurence:445 coexpression:469 experimental:721
Rv2933 ppsC phthiocerol synthesis polyketide synthase type I PpsC 931 920 ctx cooccurence:434 coexpression:471 experimental:721
Rv2048c pks12 polyketide synthase 920 908 coexpression:469 experimental:721
Rv3800c pks13 polyketide synthase 914 888 coexpression:659 experimental:473
Rv2384 mbtA 2,3-dihydroxybenzoate-AMP ligase 918 874 coexpression:685
Rv1529 fadD24 fatty-acid--CoA ligase FadD24 873 872 ctx fusion:506 cooccurence:651
Rv0405 pks6 membrane bound polyketide synthase 874 868 ctx cooccurence:510 coexpression:442 experimental:473

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): peptide synthetase
  • Pfam (hmmscan --cut_ga): Condensation PF00668.26 (E=1e-59), AMP-binding PF00501.35 (E=5e-69), AMP-binding_C PF13193.13 (E=9e-08), PP-binding PF00550.32 (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_216895.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Condensation (PF00668.26), AMP-binding (PF00501.35), AMP-binding_C (PF13193.13), PP-binding (PF00550.32)
  • 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 COG1020
  • Curated reference: UniProt O05819 (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 — 95 functional partner(s); context anchor mbtE
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv2379c|mbtF
MGPVAVTRADARGAIDDVMALSPLQQGLFSRATLVAAESGSEAAEADPYVIAMAADAAGPLDIALLRDCAAAMLTRHPNLRASFLHGNLSRPVQVIPSSAEVLWRHVRAHPSEVGALAAEERRRRFDVGRGPLIRFLLIELPDECWHLVIVAHHIVIDGWSLPLFVSELLALYRAGGHVAALPAAPRPYRDYIGWLAGRDQTASRAMWADHLNGLDGPTLLSPALADTPVQPGIPGRTEVRLDREATAELADAARTRGVTISTLVQMAWATTLSAFTGRGDVTFGVTVSGRPSELSGVETMIGLFINTVPLRVRLDARATVGGQCAVLQRQFAMLRDHSYLGFNEFRAIAGIGEMFDTLLVYENFPPGEVVGTAEFVANGVTFRPVALESLSHFPVTVAAHRSTGELTLLVEVLDGALGTMAPESLGRRVLAVLQRLVSRWDRPLRDVDILLDGEHDPTAPGLPDVTTSAPAVHTRFAEIAAAQPDSVAVSWADGQLTYRELDALADRLATGLRRADVSRETPVAVALSRGPRYVAAMLAVLKAGGMIVPLDPAMPGERVAEILRQTSAPVVIDEGVFAASVGADILEEDRAITVPVDQAAYVIFTSGTTGTPKGVIGTHRALSAYADDHIERVLRPAAQRLGRPLRIAHAWSFTFDAAWQPLVALLDGHAVHIVDDHRQRDAGALVEAIDRFGLDMIDTTPSMFAQLHNAGLLDRAPLAVLALGGEALGAATWRMIQQNCARTAMTAFNCYGPTETTVEAVVAAVAEHARPVIGRPTCTTRAYVMDSWLRPVPDGVAGELYLAGAQLTRGYLGRPAETAARFVAEPNGRGSRMYRTGDVVRRLPDGGLEFLGRSDDQVKIRGFRVEPGEIAAVLNGHHAVHGCHVTARGHASGPRLTAYVAGGPQPPPVAELRAMLLERLPRYLVPHHIVVLDELPLTPHGKIDENALAAINVTEGPATPPQTPTELVLAEAFADVMETSNVDVTAGFLQMGLDSIVALSVVQAARRRGIALRARLMVECDTIRELAAAIDSDAAWQAPANDAGEPIPVLPNTHWLYEYGDPRRLAQTEVIRLPDRITRERLDAVLAAVVDGHEVLRCRFDRDAMALVAQPKTDILSEVWVSGELVTAVAEQTLGALASLDPQAGRLLSAVWLREPDGPGVLVLTAHVLAMDPASWRIVLGELDAGLHALAAGRAPSPARENTSYRQWSRLLAQRAKALDSVDFWVAELEGADPPLGARRVAPQTDRVGELAITMSISDADLTARLLSTGRSMTDLLATAAARMVTAWRRQRGQQTPAPLLALETHGRADVHVDKTADTSDTVGLLSAIYPLRIHCDGATDFARIPGSGIDYGLLRYLRADTAERLRAHREPQLLLNYLGSLHVGVGDLAVDRALLADVGQLPEPEQPVRHELTVLAALLGPADAPVLATRWRTLPDILSADDVATLQSLWQGALAEITA