Structure of SixA, a Histidine Protein Phosphatase of the ArcB Histidine‐Containing Phosphotransfer Domain in Escherichia coli

Hakoshima, Toshio; Ichihara, Hisako

doi:10.1016/s0076-6879(06)22014-7

Cited by 7 publications

(6 citation statements)

References 27 publications

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“…Our results also revealed that during the dephosphorylation reaction, SixA reacts with τ-pHis antibody (Figure 3). This finding is in agreement with predictions that catalysis by SixA proceeds through a τ-pHis intermediate (38,39).…”

Section: Discussionsupporting

confidence: 92%

“…SixA homologs are distributed across many phyla and are especially well represented among Proteobacteria, Cyanobacteria, and Actinobacteria (38). Within Proteobacteria, SixA sequences tend to cluster together by taxonomic class ( Figure 5).…”

Section: Discussionmentioning

confidence: 99%

“…SixA (Signal Inhibitory factor X) is a wellconserved bacterial protein (38) belonging to the histidine phosphatase superfamily (1,39,40). The "histidine" in this superfamily name refers not to substrate specificity but rather to the conserved residue in the active site that is essential for enzyme activity and that becomes phosphorylated during catalysis.…”

Section: Introductionmentioning

confidence: 99%

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The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr

Schulte

Roggiani

Shi

et al. 2021

Journal of Biological Chemistry

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Histidine phosphorylation is a post-translational modification that alters protein function and also serves as an intermediate of phosphoryl transfer. Although phosphohistidine is relatively unstable, enzymatic dephosphorylation of this residue is apparently needed in some contexts, since both prokaryotic and eukaryotic phosphohistidine phosphatases have been reported. Here we identify the mechanism by which a bacterial phosphohistidine phosphatase dephosphorylates the nitrogen-related phosphotransferase system, a broadly conserved bacterial pathway that controls diverse metabolic processes. We show that the phosphatase SixA dephosphorylates the phosphocarrier protein NPr, and that the reaction proceeds through phosphoryl transfer from a histidine on NPr to a histidine on SixA. In addition, we show that Escherichia coli lacking SixA are out-competed by wild-type E. coli in the context of commensal colonization of the mouse intestine. Notably, this colonization defect requires NPr and is distinct from a previously identified in vitro growth defect associated with dysregulation of the nitrogen-related phosphotransferase system. The wide-spread conservation of SixA, and its coincidence with the phosphotransferase system studied here, suggests that this dephosphorylation mechanism may be conserved in other bacteria.

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Section: Discussionsupporting

confidence: 92%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr

Schulte

Roggiani

Shi

et al. 2021

Journal of Biological Chemistry

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“…SixA is a well-conserved protein found in proteobacteria, actinobacteria, and cyanobacteria ( 5 ). Gene expression and proteome analyses have implicated SixA in biofilms of E. coli and Acidithiobacillus ferrooxidans ( 42 – 45 ), in nutrient limitation-induced phenotypes of Legionella and Salmonella ( 46 – 48 ), and macrophage infection with Salmonella ( 38 ).…”

Section: Discussionmentioning

confidence: 99%

“…As of this writing, all E. coli isolates with fully sequenced genomes contain sixA , making it a member of the E. coli core genome. In addition, homologs of sixA are widespread among proteobacteria, actinobacteria, and cyanobacteria ( 5 ). Thus, SixA likely plays an important role in the physiology of these organisms.…”

Section: Introductionmentioning

confidence: 99%

The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System

Schulte

Goulian

2018

mBio

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One common means to regulate protein activity is through phosphorylation. Protein phosphatases exist to reverse this process, returning the protein to the unphosphorylated form. The vast majority of protein phosphatases that have been identified target phosphoserine, phosphotheronine, and phosphotyrosine. A widely conserved phosphohistidine phosphatase was identified in Escherichia coli 20 years ago but remains relatively understudied. The present work shows that this phosphatase modulates the nitrogen-related phosphotransferase system, a pathway that is regulated by nitrogen and carbon metabolism and affects diverse aspects of bacterial physiology. Until now, there was no known mechanism for removing phosphoryl groups from this pathway.

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Protein Phosphohistidine Phosphatases of the HP Superfamily

Rigden¹

2019

Methods in Molecular Biology

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Structure of SixA, a Histidine Protein Phosphatase of the ArcB Histidine‐Containing Phosphotransfer Domain in Escherichia coli

Cited by 7 publications

References 27 publications

The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr

The phosphohistidine phosphatase SixA dephosphorylates the phosphocarrier NPr

The Phosphohistidine Phosphatase SixA Targets a Phosphotransferase System

Protein Phosphohistidine Phosphatases of the HP Superfamily

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