groES Resolved · high auto-curated

H37Rv Rv3418c · MTBC0 - · 100 aa · 3836986–3837288 (-) · RefSeq NP_217935.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)chaperonin GroES
MTBC0 PGAP re-annotation
Revised (this work)Chaperonin GroES. Pfam: Cpn10 (PF00166.27).

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 P9WPE5 SwissProt · reviewed · Evidence at protein level
UniProt nameCo-chaperonin GroES
Curated functionTogether with the chaperonin GroEL, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding. GroES binds to the apical surface of the GroEL ring, thereby capping the opening of the GroEL channel.

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category O Post-translational modification, protein turnover, chaperones
Preferred namegroS
eggNOG descriptionBinds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter
Orthologous groupCOG0234
KEGG orthology K04078
Gene Ontology (63) GO:0003674, GO:0005488, GO:0005515, GO:0005575, GO:0005576, GO:0005618, GO:0005622, GO:0005623, GO:0005737, GO:0005829, GO:0005886, GO:0006355 +51 more

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) 1 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
Cpn10PF00166.27 7.8e-365–98 Chaperonin 10 Kd subunit

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

Closest characterised functional partner: groEL1 (chaperonin GroEL), high confidence from genomic context alone (score 998 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3417c groEL1 chaperonin GroEL 999 998 ctx neighborhood:776 cooccurence:772 coexpression:831 experimental:829 textmining:953
Rv0440 groEL2 molecular chaperone GroEL 999 998 ctx cooccurence:772 coexpression:960 experimental:829 textmining:938
Rv0351 grpE stress response protein GrpE 984 913 coexpression:893 textmining:828
Rv0350 dnaK chaperone protein DnaK 988 812 coexpression:743 textmining:939
Rv2299c htpG chaperone protein HtpG 954 797 coexpression:769 textmining:785
Rv2460c clpP2 ATP-dependent CLP protease proteolytic subunit 2 870 761 ctx cooccurence:434 experimental:420 textmining:481
Rv2264c hyp hypothetical protein 824 759 coexpression:671
Rv3446c hyp hypothetical protein 824 759 coexpression:670
Rv0312 hyp hypothetical protein 824 759 coexpression:671
Rv2461c clpP1 ATP-dependent CLP protease proteolytic subunit 1 874 744 experimental:420 textmining:530
Rv0652 rplL 50S ribosomal protein L7/L12 830 702 coexpression:648 textmining:454
Rv3147 nuoC NADH-quinone oxidoreductase subunit C 695 664 database:604
Rv0352 dnaJ1 chaperone protein DnaJ 872 644 coexpression:577 textmining:656
Rv3419c gcp O-sialoglycoprotein endopeptidase 758 627 ctx neighborhood:576
Rv0070c glyA2 serine hydroxymethyltransferase 640 620 database:546

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): chaperonin GroES
  • Pfam (hmmscan --cut_ga): Cpn10 PF00166.27 (E=8e-36)
  • (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_217935.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Cpn10 (PF00166.27)
  • 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 COG0234
  • Curated reference: UniProt P9WPE5 (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 — 138 functional partner(s); context anchor groEL1
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>H37Rv|Rv3418c|groES
MAKVNIKPLEDKILVQANEAETTTASGLVIPDTAKEKPQEGTVVAVGPGRWDEDGEKRIPLDVAEGDTVIYSKYGGTEIKYNGEEYLILSARDVLAVVSK