Annotation: from legacy to revised
| Legacy (H37Rv / Mycobrowser) | cutinase |
|---|
| MTBC0 PGAP re-annotation | cutinase Cfp21 |
|---|
| Revised (this work) | Cutinase Cfp21. Pfam: Cutinase (PF01083.29). |
|---|
Auto-curated: this verdict and function were generated by rules from
PGAP + Pfam + Foldseek and have not been hand-reviewed.
Curated reference (UniProt)
| UniProt |
P9WP43
SwissProt · reviewed
· Evidence at protein level
|
|---|
| UniProt name | Carboxylesterase Culp1 |
|---|
| EC (curated) |
EC 3.1.1.-
|
|---|
| Curated function | Shows esterase activity, with a preference for short- and medium-chain fatty acids. Also has weak lipase activity, but does not exhibit cutinase activity. Hydrolyzes various p-nitrophenol-linked aliphatic esters, including pNP-butyrate (C4), pNP-valerate (C5), pNP-hexanoate (C6), pNP-octanoate (C8) and pNP-decanoate (C10). Can use pNP-laurate (C12) and pNP-myristate (C14), with lower efficiency. Can also hydrolyze monocaprylin and triolein, with a slow turnover..; FUNCTION: Induces a strong delayed-type hypersensitivity (DTH) response in animal model of tuberculosis, cellular and humoral immun. |
|---|
Functional vocabulary (eggNOG-mapper, orthology transfer)
| COG category |
M Cell wall / membrane / envelope biogenesis
|
|---|
| Preferred name | cfp21 |
|---|
| eggNOG description | Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle |
|---|
| Orthologous group | 2A1QU |
|---|
| EC number |
EC 3.1.1.74
|
|---|
| KEGG orthology |
K08095
|
|---|
| Gene Ontology (51) |
GO:0003674, GO:0003824, GO:0005575, GO:0005576, GO:0005618, GO:0005623, GO:0006082, GO:0006629, GO:0006631, GO:0006638, GO:0006639, GO:0008150 +39 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 |
1.032 · relaxed/neutral
|
|---|
| Polymorphic sites (≥ 0.1% of strains) |
1 synonymous, 3 missense, 0 nonsense, 2 frameshift
|
|---|
| Disruption |
2 distinct premature-stop/frameshift site(s); most common in
0.74% of strains
(1081) · clonal
|
|---|
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 |
|---|
Cutinase | PF01083.29 |
4.8e-61 | 34–213 |
Cutinase |
Functional interaction network (STRING v12, guilt-by-association)
| Partner | Product | Score | No text-mining | Channels (≥400) |
|---|
Rv1592c hyp |
hypothetical protein |
636 |
636 ctx |
cooccurence:633 |
Rv0888 spmT hyp |
hypothetical protein |
466 |
466 ctx |
cooccurence:463 |
Rv2672 |
protease |
466 |
332 |
|
Rv3802c |
membrane protein |
833 |
188 |
textmining:803 |
Rv2537c aroD |
3-dehydroquinate dehydratase |
481 |
155 |
textmining:411 |
Rv1981c nrdF1 |
ribonucleoside-diphosphate reductase subunit beta NrdF1 |
519 |
59 |
textmining:510 |
Rv1980c mpt64 |
immunogenic protein Mpt64 |
809 |
51 |
textmining:807 |
Rv1886c fbpB |
diacylglycerol acyltransferase/mycolyltransferase Ag85B |
630 |
51 |
textmining:627 |
Rv3875 esxA |
ESAT-6 protein EsxA |
515 |
49 |
textmining:511 |
Rv3874 esxB |
ESAT-6-like protein EsxB |
648 |
47 |
textmining:646 |
Rv2785c rpsO |
30S ribosomal protein S15 |
492 |
47 |
textmining:489 |
Rv3400 |
hydrolase |
442 |
47 |
textmining:439 |
Rv2031c hspX |
alpha-crystallin |
406 |
47 |
textmining:403 |
Rv3724A cut5a |
Rv3724A, (MTV025.072), len: 80 aa. Probable cut5a,truncated cutinase precursor, similar to N-terminal end of others e.g. Q9KK87 serine ester |
543 |
46 |
textmining:541 |
Rv1263 amiB2 |
amidase AmiB |
518 |
46 |
textmining:516 |
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: cutinase
- MTBC0 PGAP product: cutinase Cfp21
- Pfam (hmmscan --cut_ga): Cutinase PF01083.29 (E=5e-61)
- (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_216500.1)
- Domains: Pfam-A via hmmscan --cut_ga — Cutinase (PF01083.29)
- 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
2A1QU
- Curated reference: UniProt
P9WP43
(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 —
20 functional partner(s)
- Primary literature: none located yet; annotation rests on the domain/homology sources above.
Ancestral MTBC0 protein sequence
>mtbc0_002107|Rv1984c|cfp21
MTPRSLVRIVGVVVATTLALVSAPAGGRAAHADPCSDIAVVFARGTHQASGLGDVGEAFVDSLTSQVGGRSIGVYAVNYPASDDYRASASNGSDDASAHIQRTVASCPNTRIVLGGYSQGATVIDLSTSAMPPAVADHVAAVALFGEPSSGFSSMLWGGGSLPTIGPLYSSKTINLCAPDDPICTGGGNIMAHVSYVQSGMTSQAATFAANRLDHAG
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