pepR Family assigned · medium auto-curated

H37Rv Rv2782c · MTBC0 mtbc0_002961 · 438 aa · 3111460–3112776 (-) · RefSeq NP_217298.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)zinc protease
MTBC0 PGAP re-annotationpitrilysin family protein
Revised (this work)Pitrilysin family protein. Pfam: Peptidase_M16 (PF00675.26), Peptidase_M16_C (PF05193.27).

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

Curated reference (UniProt)

UniProt P9WHT5 SwissProt · reviewed · Evidence at protein level
UniProt nameUncharacterized zinc protease Rv2782c
EC (curated) EC 3.4.24.-

UniProt still lists this protein as Uncharacterized zinc protease Rv2782c; the revised annotation above is ahead of the current UniProt record.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category S Function unknown
Preferred namepepR
eggNOG descriptionBelongs to the peptidase M16 family
Orthologous groupCOG0612
Gene Ontology (6) GO:0005575, GO:0005623, GO:0005886, GO:0016020, 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 2.56 · diversifying/relaxed
Polymorphic sites (≥ 0.1% of strains) 2 synonymous, 14 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
Peptidase_M16PF00675.26 8.6e-3725–171 Insulinase (Peptidase family M16)
Peptidase_M16_CPF05193.27 4.4e-42179–354 Peptidase M16 inactive domain

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

Closest characterised functional partner: gpsI (bifunctional guanosine pentaphosphate synthetase/polyribonucleotide nucleotidyltransferase), high confidence from genomic context alone (score 941 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv2195 qcrA ubiquinol-cytochrome C reductase rieske iron-sulfur subunit 997 996 coexpression:710 experimental:928 database:844
Rv2196 qcrB ubiquinol-cytochrome C reductase cytochrome subunit B 989 989 experimental:928 database:844
Rv3150 nuoF NADH-quinone oxidoreductase subunit F 977 974 coexpression:701 experimental:917
Rv3151 nuoG NADH-quinone oxidoreductase subunit G 974 971 coexpression:665 experimental:916
Rv3153 nuoI NADH-quinone oxidoreductase subunit I 973 971 coexpression:652 experimental:915
Rv3149 nuoE NADH-quinone oxidoreductase subunit E 969 968 coexpression:638 experimental:915
Rv3148 nuoD NADH-quinone oxidoreductase subunit D 963 956 coexpression:595 experimental:895
Rv0310c hyp hypothetical protein 956 950 coexpression:409 experimental:919
Rv3147 nuoC NADH-quinone oxidoreductase subunit C 947 942 coexpression:489 experimental:891
Rv2783c gpsI bifunctional guanosine pentaphosphate synthetase/polyribonucleotide nucleotidyltransferase 945 941 ctx neighborhood:882
Rv3146 nuoB NADH-quinone oxidoreductase subunit B 938 933 experimental:894
Rv2200c ctaC cytochrome C oxidase subunit II 930 923 experimental:919
Rv2193 ctaE cytochrome C oxidase subunit III 926 922 experimental:915
Rv3043c ctaD cytochrome C oxidase cytochrome 1 929 920 experimental:917
Rv3157 nuoM NADH-quinone oxidoreductase subunit M 892 886 experimental:882

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: zinc protease
  • MTBC0 PGAP product: pitrilysin family protein
  • Pfam (hmmscan --cut_ga): Peptidase_M16 PF00675.26 (E=9e-37), Peptidase_M16_C PF05193.27 (E=4e-42)
  • (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_217298.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Peptidase_M16 (PF00675.26), Peptidase_M16_C (PF05193.27)
  • 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 COG0612
  • Curated reference: UniProt P9WHT5 (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 — 135 functional partner(s); context anchor gpsI
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_002961|Rv2782c|pepR
MPRRSPADPAAALAPRRTTLPGGLRVVTEFLPAVHSASVGVWVGVGSRDEGATVAGAAHFLEHLLFKSTPTRSAVDIAQAMDAVGGELNAFTAKEHTCYYAHVLGSDLPLAVDLVADVVLNGRCAADDVEVERDVVLEEIAMRDDDPEDALADMFLAALFGDHPVGRPVIGSAQSVSVMTRAQLQSFHLRRYTPERMVVAAAGNVDHDGLVALVREHFGSRLVRGRRPVAPRKGTGRVNGSPRLTLVSRDAEQTHVSLGIRTPGRGWEHRWALSVLHTALGGGLSSRLFQEVRETRGLAYSVYSALDLFADSGALSVYAACLPERFADVMRVTADVLESVARDGITEAECGIAKGSLRGGLVLGLEDSSSRMSRLGRSELNYGKHRSIEHTLRQIEQVTVEEVNAVARHLLSRRYGAAVLGPHGSKRSLPQQLRAMVG