pepD Resolved · high auto-curated

H37Rv Rv0983 · MTBC0 mtbc0_001054 · 464 aa · 1106402–1107796 (+) · RefSeq NP_215498.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)serine protease PepD
MTBC0 PGAP re-annotationserine protease PepD
Revised (this work)Serine protease PepD. Pfam: Trypsin (PF00089.33), Trypsin_2 (PF13365.13), PDZ (PF00595.30), PDZ_2 (PF13180.13).

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

Curated reference (UniProt)

UniProt O53896 SwissProt · reviewed · Evidence at protein level
UniProt nameSerine protease PepD
EC (curated) EC 3.4.21.107
Curated functionRequired for virulence. Acts both as a protease, which degrades and/or refolds damaged substrate targets, and as a chaperone. Plays an important role in the stress response network mediated through the two-component regulatory system MprAB and SigE signaling networks. May utilize its PDZ domain to recognize and process misfolded proteins at the cell membrane, leading to activation of the MprAB and SigE signaling pathways and subsequent establishment of a positive feedback loop that facilitates bacterial adaptation. Interacts with and potentially cleaves several proteins, including the 35 kDa a.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category O Post-translational modification, protein turnover, chaperones
Preferred namepepD
eggNOG descriptionCOG0265 Trypsin-like serine proteases, typically periplasmic, contain C-terminal PDZ domain
Orthologous groupCOG0265
KEGG orthology K08372
KEGG pathways map02020

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 0.204 · purifying
Polymorphic sites (≥ 0.1% of strains) 9 synonymous, 5 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
TrypsinPF00089.33 7.1e-16180–359 Trypsin
Trypsin_2PF13365.13 2.1e-32181–331 Trypsin-like peptidase domain
PDZPF00595.30 6.7e-06373–444 PDZ domain
PDZ_2PF13180.13 7.4e-10378–446 PDZ domain

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

Closest characterised functional partner: moaB2 (pterin-4-alpha-carbinolamine dehydratase), high confidence from genomic context alone (score 982 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv0984 moaB2 pterin-4-alpha-carbinolamine dehydratase 981 982 ctx neighborhood:881 coexpression:853
Rv0982 mprB two component histidine-protein kinase/phosphatase MprB 941 939 ctx neighborhood:702 coexpression:805
Rv2115c mpa proteasome-associated ATPase 831 821 experimental:551 database:594
Rv0563 htpX protease HtpX 819 810 coexpression:804
Rv0981 mprA two-component response regulator MrpA 790 776 ctx neighborhood:683
Rv2710 sigB RNA polymerase sigma factor SigB 788 771 coexpression:710
Rv2711 ideR iron-dependent repressor and activator IdeR 761 762 coexpression:757
Rv3837c phosphoglycerate mutase 760 761 coexpression:757
Rv2051c ppm1 polyprenol-monophosphomannose synthase 769 759 coexpression:730
Rv3696c glpK glycerol kinase 767 753 experimental:402 database:589
Rv2053c fxsA transmembrane protein FxsA 740 741 coexpression:732
Rv1334 mec [CysO 721 712 database:576
Rv2109c prcA proteasome subunit alpha 645 628 database:562
Rv2110c prcB proteasome subunit beta 643 626 database:562
Rv2555c alaS alanine--tRNA ligase 639 626 database:586

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: serine protease PepD
  • MTBC0 PGAP product: serine protease PepD
  • Pfam (hmmscan --cut_ga): Trypsin PF00089.33 (E=7e-16), Trypsin_2 PF13365.13 (E=2e-32), PDZ PF00595.30 (E=7e-06), PDZ_2 PF13180.13 (E=7e-10)
  • (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_215498.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Trypsin (PF00089.33), Trypsin_2 (PF13365.13), PDZ (PF00595.30), PDZ_2 (PF13180.13)
  • 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 COG0265
  • Curated reference: UniProt O53896 (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 — 246 functional partner(s); context anchor moaB2
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_001054|Rv0983|pepD
MAKLARVVGLVQEEQPSDMTNHPRYSPPPQQPGTPGYAQGQQQTYSQQFDWRYPPSPPPQPTQYRQPYEALGGTRPGLIPGVIPTMTPPPGMVRQRPRAGMLAIGAVTIAVVSAGIGGAAASLVGFNRAPAGPSGGPVAASAAPSIPAANMPPGSVEQVAAKVVPSVVMLETDLGRQSEEGSGIILSAEGLILTNNHVIAAAAKPPLGSPPPKTTVTFSDGRTAPFTVVGADPTSDIAVVRVQGVSGLTPISLGSSSDLRVGQPVLAIGSPLGLEGTVTTGIVSALNRPVSTTGEAGNQNTVLDAIQTDAAINPGNSGGALVNMNAQLVGVNSAIATLGADSADAQSGSIGLGFAIPVDQAKRIADELISTGKASHASLGVQVTNDKDTPGAKIVEVVAGGAAANAGVPKGVVVTKVDDRPINSADALVAAVRSKAPGATVALTFQDPSGGSRTVQVTLGKAEQ