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Literature summary for 2.7.13.3 extracted from

  • Fukushima, T.; Furihata, I.; Emmins, R.; Daniel, R.A.; Hoch, J.A.; Szurmant, H.
    A role for the essential YycG sensor histidine kinase in sensing cell division (2011), Mol. Microbiol., 79, 503-522.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene yycG, recombinant expression of trncated enzyme mutants. Expression of a soluble cytoplasmic YycG construct in a bacterial two-hybrid expression system using the full-length YycG or a truncated YycGDELTA211-611 that lacks all cytoplasmic domains, and cell division proteins FtsZ, FtsA, FtsW, DivIB, DivIC, FtsL, Pbp2B, EzrA, ZapA, SepF and MinJ as C-terminal fusions to the individual domains (T18 and T25) of the two-domain Bordatella pertussis adenylate cyclase protein. YycG makes specific interactions with FtsL, DivIB, Pbp2B and interactions with FtsW and EzrA appear also possible Bacillus subtilis

Protein Variants

Protein Variants Comment Organism
additional information generation of several truncation mutant of enzyme YycG. All truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum. N-terminal truncations of YycG lose negative regulation of their activity, truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
YycH an extracytoplasmic membrane anchored protein. Enzyme YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI. YycG regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome Bacillus subtilis
YycI an extracytoplasmic membrane anchored protein. Enzyme YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI. YycG regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome Bacillus subtilis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell septum division septum, a cytoplasmic domain of YycG is sufficient for septum localization. All recombinant truncated YycG constructs including the shortest one that featured only the cytoplasmic PAS and the two catalytic HisKA and HATPase domains retain the ability to localize to the septum Bacillus subtilis 30428
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membrane the YycG kinase is associated in the membrane as a complex with YycH and YycI through interaction of their transmembrane domains Bacillus subtilis 16020
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Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q45614
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Bacillus subtilis 168 Q45614
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL Bacillus subtilis ?
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?
additional information YycG interacts with the latter stage cell division proteins DivIB, Pbp2B and FtsL Bacillus subtilis 168 ?
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?

Synonyms

Synonyms Comment Organism
BSU40400
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Bacillus subtilis
sensor histidine kinase
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Bacillus subtilis
WalK
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Bacillus subtilis
YycG
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Bacillus subtilis
YycG kinase
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Bacillus subtilis

General Information

General Information Comment Organism
malfunction N-terminal truncations of YycG lose negative regulation of their activity, phenotypes, overview. Truncated YycG constructs fail to co-immunoprecipitate with the regulatory proteins YycH and YycI. Deletion or depletion of later stage cell division proteins does not perturb YycG localization Bacillus subtilis
physiological function The enzyme YycG is part of the two-component signal transduction system YycFG or WalRK. The YycG (WalK) sensor histidine kinase coordinates cell wall remodeling with cell division in Gram-positive bacteria by controlling the transcription of genes for autolysins and their inhibitors. The essential enzyme YycG senses cell division and is enzymatically activated by associating with the divisome at the division septum. The cytoplasmic PAS domain of this multidomain trans-membrane kinase is a determining factor translocating the kinase to the division septum. YycG activity in non-dividing cells is suppressed by its interaction with YycH and YycI and its activation is coordinated to cell division in dividing cells by specific interactions that occur within the divisome. This regulation is accomplished through its transmembrane and extra-membrane domains interacting with the membrane associated YycH and YycI proteins that do not localize to the divisome. Signaling by YycG involves later stage cell division proteins, overview Bacillus subtilis