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Links from Protein

Items: 12

1.

Histidine kinase sensor domain

The Bacillus subtilis ResD-ResE two-component (TC) regulatory system activates genes involved in nitrate respiration in response to oxygen limitation or nitric oxide (NO). The sensor kinase ResE activates the response regulator ResD through phosphorylation, which then binds to the regulatory region of genes involved in anaerobiosis to activate their transcription. In other words, ResE is involved in sensing signals related to the redox state of the cells. ResE is composed of an N-terminal signal input domain and a C-terminal catalytic domain. The N-terminal domain contains two transmembrane subdomains and a large extra-cytoplasmic loop. Mutational analysis indicate that cytoplasmic ResE lacking the transmembrane segments and the extra-cytoplasmic loop retains the ability to sense oxygen limitation and NO, which leads to transcriptional activation of ResDE-dependent genes. Having said that, it is also proposed that the extra-cytoplasmic region may serve as a second signal-sensing subdomain. This suggests that the extracytoplasmic region could contribute to amplification of ResE activity leading to the robust activation of genes required for anaerobic metabolism in B. subtilis. This entry represents the extracytoplasmic subdomain [1]. Family members also include SrrB found in S. aureus that is similar to ResE of B. subtilis [2]. [1]. 14996800. Mutational analysis of the signal-sensing domain of ResE. histidine kinase from Bacillus subtilis.. Baruah A, Lindsey B, Zhu Y, Nakano MM;. J Bacteriol. 2004;186:1694-1704.. [2]. 27512901. Bacterial Stress Responses during Host Infection.. Fang FC, Frawley ER, Tapscott T, Vazquez-Torre. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-08-14
Family Accession:
NF037391.5
Method:
HMM
2.

ATP-binding protein

This family represents the structurally related ATPase domains of histidine kinase, DNA gyrase B and HSP90. [1]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from. Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray. source.. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng. C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu. ZJ;. Proteins 2008;71:2109-13. (from Pfam)

Date:
2024-08-14
Family Accession:
NF014567.5
Method:
HMM
3.

HAMP domain-containing protein

GO Terms:
Biological Process:
signal transduction (GO:0007165)
Cellular Component:
membrane (GO:0016020)
Date:
2024-08-14
Family Accession:
NF012876.5
Method:
HMM
4.

histidine kinase dimerization/phospho-acceptor domain-containing protein

Dimerisation and phospho-acceptor domain of histidine kinases. [1]. 9989504. Structure of CheA, a signal-transducing histidine kinase.. Bilwes AM, Alex LA, Crane BR, Simon MI;. Cell 1999;96:131-141.. [2]. 18361456. Crystal structure of a novel non-Pfam protein AF1514 from. Archeoglobus fulgidus DSM 4304 solved by S-SAD using a Cr X-ray. source.. Li Y, Bahti P, Shaw N, Song G, Chen S, Zhang X, Zhang M, Cheng. C, Yin J, Zhu JY, Zhang H, Che D, Xu H, Abbas A, Wang BC, Liu. ZJ;. Proteins 2008;71:2109-13. (from Pfam)

GO Terms:
Molecular Function:
phosphorelay sensor kinase activity (GO:0000155)
Biological Process:
signal transduction (GO:0007165)
Date:
2024-08-14
Family Accession:
NF012722.5
Method:
HMM
5.
new record, indexing in progress
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6.
new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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new record, indexing in progress
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11.
new record, indexing in progress
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12.
new record, indexing in progress
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