Evidence map›Paper›PMID 41506723›Full record

ArticleThe FEBS journal2026

A Hanks-type bacterial kinase, PknS, directly phosphorylates the alternative sigma factor EcfK to promote resistance to protist predation.

Lídia Dos Passos Lima, Dev Sriranganadane, Daiane Laise da Silva, Natália C Drebes Dörr, Enzo Breviglieri Sichi Mello, Caio Vinicius Dos Reis, Rogério Ferreira Lourenço, José Felipe Teixeira da Silva Santos, Anita Salmazo, Brenno Wendler Miranda and 3 more

Abstract read
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In one paragraph

Article in The FEBS journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

13 authors.

Lídia Dos Passos LimaDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
Dev SriranganadaneCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.
Daiane Laise da SilvaCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.
Natália C Drebes DörrDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
Enzo Breviglieri Sichi MelloDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
Caio Vinicius Dos ReisCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.
Rogério Ferreira LourençoDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
José Felipe Teixeira da Silva SantosDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
Anita SalmazoCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.
Brenno Wendler MirandaDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.
Katlin B MassirerCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.
Rafael M CouñagoCentro de Química Medicinal (CQMED), Centro de Biologia Molecular e Engenharia Genética (CBMEG), Universidade Estadual de Campinas (UNICAMP), Brazil.ORCID 0000-0003-1847-5090
Cristina E Alvarez-MartinezDepartamento de Genética, Evolução, Microbiologia e Imunologia, Instituto de Biologia, Universidade Estadual de Campinas (UNICAMP), Brazil.ORCID 0000-0003-3882-1835

Funding

Conselho Nacional de Desenvolvimento Científico e Tecnológico 107899/2024-8Conselho Nacional de Desenvolvimento Científico e Tecnológico 351211/2024-1Conselho Nacional de Desenvolvimento Científico e Tecnológico 465651/2014-3Coordenação de Aperfeiçoamento de Pessoal de Nível Superior 001Coordenação de Aperfeiçoamento de Pessoal de Nível Superior 88887.146077/2017-00Fundação de Amparo à Pesquisa do Estado de São Paulo 2014/50897-0Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/10577-0Fundação de Amparo à Pesquisa do Estado de São Paulo 2021/12236-5Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/06555-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/11998-1Fundação de Amparo à Pesquisa do Estado de São Paulo 2022/15160-2Fundação de Amparo à Pesquisa do Estado de São Paulo 2023/05679-3Fundação de Amparo à Pesquisa do Estado de São Paulo 2024/22005-9Fundação de Amparo à Pesquisa do Estado de São Paulo 2024/22312-9Fundação de Desenvolvimento da Unicamp 4992Fundo de Apoio ao Ensino, à Pesquisa e Extensão, Universidade Estadual de Campinas
6 · The paper itself

Abstract

Serine/threonine (Ser/Thr) kinases of the Hanks-type family are widespread in bacteria, playing key roles in signal transduction. The transmembrane Ser/Thr kinase PknS (XAC4127) from the phytopathogenic bacterium Xanthomonas citri is required for the expression of a type VI secretion system, which confers resistance to predation by the soil amoeba Dictyostelium discoideum. PknS exerts its function via activation of the cognate ECF-type alternative sigma factor EcfK, ultimately triggering the expression of type VI secretion system (T6SS) genes. In this study, we characterize PknS, demonstrating its ability to undergo autophosphorylation both in vitro and within X. citri cells. Structural analysis of the PknS kinase domain revealed the conservation of the canonical fold characteristic of Hanks-type kinases. PknS directly phosphorylates EcfK at five Ser/Thr residues located in two distinct regions of the sigma factor: the conserved σ

Indexed as

Bacterial ProteinsProtein Serine-Threonine KinasesSigma FactorXanthomonasAmino Acid SequenceDictyosteliumModels, MolecularPhosphorylationProtein DomainsSignal TransductionType VI Secretion SystemsBacterial ProteinsProtein Serine-Threonine KinasesSigma FactorType VI Secretion Systemsamoeba predationkinasesigma factor regulationtype VI secretion systemXanthomonas

Identifiers

PMID41506723
PMCPMC13147305

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.