fusA1 Resolved · high auto-curated
H37Rv Rv0684 · MTBC0 - ·
701 aa · 782485–784590 (+) ·
RefSeq YP_177746.1
Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | elongation factor G |
|---|---|
| MTBC0 PGAP re-annotation | — |
| Revised (this work) | Elongation factor G. Pfam: GTP_EFTU (PF00009.34), EF-G_D2 (PF22042.3), GTP_EFTU_D2 (PF03144.32), EFG_III (PF14492.13), EFG_IV (PF03764.25), EFG_C (PF00679.31). |
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 |
P9WNM7
SwissProt · reviewed
· Evidence at protein level
|
|---|---|
| UniProt name | Elongation factor G |
| Curated function | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). |
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
J Translation, ribosomal structure and biogenesis
|
|---|---|
| Preferred name | fusA |
| eggNOG description | Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome |
| Orthologous group | COG0480 |
| KEGG orthology |
K02355
|
| Gene Ontology (10) |
GO:0005575, GO:0005618, GO:0005623, GO:0005886, GO:0008150, GO:0016020, GO:0030312, GO:0040007, 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 | 0.044 · strong purifying |
|---|---|
| Polymorphic sites (≥ 0.1% of strains) | 14 synonymous, 2 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 |
|---|---|---|---|---|
GTP_EFTU | PF00009.34 | 3.0e-65 | 12–285 | Elongation factor Tu GTP binding domain |
EF-G_D2 | PF22042.3 | 3.9e-15 | 313–395 | Elongation factor G domain 2 |
GTP_EFTU_D2 | PF03144.32 | 3.3e-16 | 328–394 | Elongation factor Tu domain 2 |
EFG_III | PF14492.13 | 2.2e-33 | 408–482 | Elongation Factor G, domain III |
EFG_IV | PF03764.25 | 3.0e-45 | 483–604 | Elongation factor G, domain IV |
EFG_C | PF00679.31 | 5.3e-30 | 608–692 | Elongation factor G C-terminus |
Functional interaction network (STRING v12, guilt-by-association)
Closest characterised functional partner: rpsG (30S ribosomal protein S7), high confidence from genomic context alone (score 1000 excluding text-mining).
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|---|---|---|---|
Rv0683 rpsG |
30S ribosomal protein S7 | 999 | 1000 ctx | neighborhood:784 cooccurence:722 coexpression:943 experimental:829 textmining:861 |
Rv0682 rpsL |
30S ribosomal protein S12 | 999 | 1000 ctx | neighborhood:784 cooccurence:695 coexpression:945 experimental:829 textmining:783 |
Rv0704 rplB |
50S ribosomal protein L2 | 999 | 998 ctx | cooccurence:707 coexpression:949 experimental:829 textmining:776 |
Rv0702 rplD |
50S ribosomal protein L4 | 998 | 998 ctx | cooccurence:622 coexpression:945 experimental:829 |
Rv0685 tuf |
elongation factor Tu | 998 | 997 ctx | neighborhood:728 coexpression:937 experimental:778 textmining:642 |
Rv0701 rplC |
50S ribosomal protein L3 | 997 | 997 ctx | cooccurence:627 coexpression:938 experimental:829 |
Rv0714 rplN |
50S ribosomal protein L14 | 998 | 996 ctx | cooccurence:560 coexpression:924 experimental:829 textmining:570 |
Rv0716 rplE |
50S ribosomal protein L5 | 997 | 996 ctx | cooccurence:547 coexpression:912 experimental:829 textmining:440 |
Rv0719 rplF |
50S ribosomal protein L6 | 997 | 996 | coexpression:951 experimental:829 textmining:406 |
Rv0700 rpsJ |
30S ribosomal protein S10 | 997 | 996 ctx | cooccurence:432 coexpression:944 experimental:829 |
Rv0705 rpsS |
30S ribosomal protein S19 | 996 | 996 ctx | cooccurence:463 coexpression:931 experimental:829 |
Rv0718 rpsH |
30S ribosomal protein S8 | 996 | 996 | coexpression:943 experimental:829 |
Rv3460c rpsM |
30S ribosomal protein S13 | 996 | 995 ctx | cooccurence:555 coexpression:931 experimental:773 |
Rv3458c rpsD |
30S ribosomal protein S4 | 996 | 995 | coexpression:930 experimental:829 |
Rv0715 rplX |
50S ribosomal protein L24 | 995 | 995 | coexpression:943 experimental:829 |
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): elongation factor G
- Pfam (hmmscan --cut_ga): GTP_EFTU PF00009.34 (E=3e-65), EF-G_D2 PF22042.3 (E=4e-15), GTP_EFTU_D2 PF03144.32 (E=3e-16), EFG_III PF14492.13 (E=2e-33), EFG_IV PF03764.25 (E=3e-45), EFG_C PF00679.31 (E=5e-30)
- (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 YP_177746.1)
- Domains: Pfam-A via hmmscan --cut_ga — GTP_EFTU (PF00009.34), EF-G_D2 (PF22042.3), GTP_EFTU_D2 (PF03144.32), EFG_III (PF14492.13), EFG_IV (PF03764.25), EFG_C (PF00679.31)
- 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
COG0480 - Curated reference: UniProt P9WNM7 (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 —
262 functional partner(s); context anchor
rpsG - Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>H37Rv|Rv0684|fusA1 MAQKDVLTDLSRVRNFGIMAHIDAGKTTTTERILYYTGINYKIGEVHDGAATMDWMEQEQERGITITSAATTTFWKDNQLNIIDTPGHVDFTVEVERNLRVLDGAVAVFDGKEGVEPQSEQVWRQADKYDVPRICFVNKMDKIGADFYFSVRTMGERLGANAVPIQLPVGAEADFEGVVDLVEMNAKVWRGETKLGETYDTVEIPADLAEQAEEYRTKLLEVVAESDEHLLEKYLGGEELTVDEIKGAIRKLTIASEIYPVLCGSAFKNKGVQPMLDAVVDYLPSPLDVPPAIGHAPAKEDEEVVRKATTDEPFAALAFKIATHPFFGKLTYIRVYSGTVESGSQVINATKGKKERLGKLFQMHSNKENPVDRASAGHIYAVIGLKDTTTGDTLSDPNQQIVLESMTFPDPVIEVAIEPKTKSDQEKLSLSIQKLAEEDPTFKVHLDSETGQTVIGGMGELHLDILVDRMRREFKVEANVGKPQVAYKETIKRLVQNVEYTHKKQTGGSGQFAKVIINLEPFTGEEGATYEFESKVTGGRIPREYIPSVDAGAQDAMQYGVLAGYPLVNLKVTLLDGAYHEVDSSEMAFKIAGSQVLKKAAALAQPVILEPIMAVEVTTPEDYMGDVIGDLNSRRGQIQAMEERAGARVVRAHVPLSEMFGYVGDLRSKTQGRANYSMVFDSYSEVPANVSKEIIAKATGE