bcp Resolved · high auto-curated
H37Rv Rv2521 · MTBC0 mtbc0_002685 ·
157 aa · 2860574–2861047 (+) ·
RefSeq NP_217037.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | peroxiredoxin |
|---|---|
| MTBC0 PGAP re-annotation | thioredoxin-dependent thiol peroxidase |
| Revised (this work) | Thioredoxin-dependent thiol peroxidase. Pfam: AhpC-TSA (PF00578.28), Redoxin (PF08534.17). |
Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.
Curated reference (UniProt)
| UniProt |
P9WIE1
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | Putative peroxiredoxin Rv2521 |
| EC (curated) |
EC 1.11.1.24
|
| Curated function | Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. |
UniProt still lists this protein as Putative peroxiredoxin Rv2521; the revised annotation above is ahead of the current UniProt record.
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
O Post-translational modification, protein turnover, chaperones
|
|---|---|
| Preferred name | bcp |
| eggNOG description | Peroxiredoxin |
| Orthologous group | COG1225 |
| EC number |
EC 1.11.1.15
|
| KEGG orthology |
K03564
|
| Gene Ontology (11) |
GO:0005575, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0016020, GO:0044424, GO:0044444, 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)
| pN/pS | 0.172 · strong purifying |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 2 synonymous, 1 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)
| Pfam | Accession | i-Evalue | Residues | Description |
|---|---|---|---|---|
AhpC-TSA | PF00578.28 | 3.9e-43 | 9–136 | AhpC/TSA family |
Redoxin | PF08534.17 | 1.5e-28 | 9–151 | Redoxin |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: Rv2520c (membrane protein), high confidence from genomic context alone (score 784 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv2520c |
membrane protein | 783 | 784 ctx | neighborhood:781 |
Rv2428 ahpC |
alkyl hydroperoxide reductase subunit AhpC | 590 | 557 ctx | cooccurence:467 |
Rv1229c mrp |
multiple resistance/pH adaptation protein | 411 | 374 | |
Rv3754 tyrA |
prephenate dehydrogenase TyrA | 402 | 348 | |
Rv3914 trxC |
thioredoxin TrxC | 710 | 209 | textmining:649 |
Rv1471 trxB1 |
thioredoxin | 630 | 206 | textmining:553 |
Rv1324 |
thioredoxin | 415 | 206 | |
Rv1470 trxA |
thioredoxin TrxA | 431 | 201 | |
Rv3913 trxB2 |
thioredoxin reductase | 490 | 100 | textmining:457 |
Rv1329c dinG |
ATP-dependent helicase DinG | 649 | 41 | textmining:649 |
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: peroxiredoxin
- MTBC0 PGAP product: thioredoxin-dependent thiol peroxidase
- Pfam (hmmscan --cut_ga): AhpC-TSA PF00578.28 (E=4e-43), Redoxin PF08534.17 (E=2e-28)
- (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_217037.1)
- Domains: Pfam-A via hmmscan --cut_ga — AhpC-TSA (PF00578.28), Redoxin (PF08534.17)
- 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
COG1225 - Curated reference: UniProt P9WIE1 (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 —
10 functional partner(s); context anchor
Rv2520c - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>mtbc0_002685|Rv2521|bcp MTKTTRLTPGDKAPAFTLPDADGNNVSLADYRGRRVIVYFYPAASTPGCTKQACDFRDNLGDFTTAGLNVVGISPDKPEKLATFRDAQGLTFPLLSDPDREVLTAWGAYGEKQMYGKTVQGVIRSTFVVDEDGKIVVAQYNVKATGHVAKLRRDLSV