Rv0799c Resolved · high auto-curated

H37Rv Rv0799c · MTBC0 mtbc0_000848 · 335 aa · 895333–896340 (-) · RefSeq NP_215314.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)hypothetical protein
MTBC0 PGAP re-annotationDyp-type peroxidase
Revised (this work)Dyp-type peroxidase. Pfam: Dyp_perox_N (PF04261.19), Dyp_perox_C (PF20628.4).

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

Curated reference (UniProt)

UniProt I6Y4U9 SwissProt · reviewed · Evidence at protein level
UniProt nameDye-decolorizing peroxidase
EC (curated) EC 1.11.1.7
Curated functionCargo of a type 1 encapsulin nanocompartment in situ; this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it is almost as protective as the intact nanocompartment; its encapsulation has a modest yet significant effect on protection against oxidative stress at low pH. A heme-dependent peroxidase, it probably does not have deferrochelatase activity. Converts guaiacol and H2O2 to tetraguaiacol, also acts on 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Retains peroxidase activity when encapsulated but has .

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category P Inorganic ion transport and metabolism
eggNOG descriptionDyp-type peroxidase
Orthologous groupCOG2837
KEGG orthology K07223

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 0.0 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 4 synonymous, 0 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
Dyp_perox_NPF04261.19 8.6e-409–137 Dyp-type peroxidase, N-terminal
Dyp_perox_CPF20628.4 7.1e-63140–304 Dyp-type peroxidase, C-terminal

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

Closest characterised functional partner: pepC (M18 family aminopeptidase), high confidence from genomic context alone (score 791 excluding text-mining). This association is the citable seed of a function hypothesis for this hypothetical protein.

PartnerProductScoreNo text-miningChannels (≥400)
Rv0798c cfp29 hyp hypothetical protein 994 972 ctx neighborhood:881 cooccurence:758 textmining:803
Rv0800 pepC M18 family aminopeptidase 791 791 ctx neighborhood:788
Rv0801 hyp hypothetical protein 756 747 ctx neighborhood:744
Rv3584 lpqE lipoprotein LpqE 481 463 coexpression:419
Rv0803 purL phosphoribosylformylglycinamidine synthase 2 445 445 ctx neighborhood:442
Rv1224 tatB Sec-independent protein translocase protein TatB 822 435 coexpression:403 textmining:698
Rv2094c tatA Sec-independent protein translocase membrane-bound protein TatA 495 433 coexpression:401
Rv2093c tatC Sec-independent protein translocase transmembrane protein TatC 781 283 textmining:707
Rv0669c neutral ceramidase 879 108 textmining:870
Rv3432c gadB glutamate decarboxylase GadB 452 77 textmining:431
Rv2677c hemY protoporphyrinogen oxidase 522 49 textmining:518
Rv3607c folB dihydroneopterin aldolase 405 46 textmining:402
Rv2149c yfiH laccase domain-containing protein 439 45 textmining:437
Rv2503c scoB succinyl-CoA:3-ketoacid-CoA transferase subunit B 432 41 textmining:432

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: hypothetical protein
  • MTBC0 PGAP product: Dyp-type peroxidase
  • Pfam (hmmscan --cut_ga): Dyp_perox_N PF04261.19 (E=9e-40), Dyp_perox_C PF20628.4 (E=7e-63)
  • (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_215314.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Dyp_perox_N (PF04261.19), Dyp_perox_C (PF20628.4)
  • 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 COG2837
  • Curated reference: UniProt I6Y4U9 (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 — 14 functional partner(s); context anchor pepC
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000848|Rv0799c|
MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTLAAGSLSIGSLKGSPR