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Search results 101 to 138 out of 138 for Spx

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0.018s

Type

Details

Score

Publication

27191337 | -

First Author:	Al-Eryani Y
Year:	2016
Journal:	Proteins
Title:	Exploring structure and interactions of the bacterial adaptor protein YjbH by crosslinking mass spectrometry.
Volume:	84
Issue:	9
Pages:	1234-45

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Publication

19074380 | -

First Author:	Garg SK
Year:	2009
Journal:	J Bacteriol
Title:	The YjbH protein of Bacillus subtilis enhances ClpXP-catalyzed proteolysis of Spx.
Volume:	191
Issue:	4
Pages:	1268-77

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Publication

30982633 | -

First Author:	Awad W
Year:	2019
Journal:	Structure
Title:	Structural Basis for YjbH Adaptor-Mediated Recognition of Transcription Factor Spx.
Volume:	27
Issue:	6
Pages:	923-936.e6

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Protein Domain

IPR046404 | Adapter_SpxH

Type:

Family

Description:

This entry represents a group of proteins from Firmicutes, including ClpXP adapter protein SpxH, also known as YjbH in Bacillus subtilis. This protein is required for efficient degradation of the RNA polymerase-binding transcription factor Spx by the protease ClpXP under non-stress conditions. It is organised into a DsbA-like thioredoxin domain, a linker and a C-terminal domain reminiscent of the winged helix-turn-helix fold [, , ].

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Publication

22648387 | J:208454

First Author:	Gotoh K
Year:	2012
Journal:	Diabetes
Title:	A novel anti-inflammatory role for spleen-derived interleukin-10 in obesity-induced inflammation in white adipose tissue and liver.
Volume:	61
Issue:	8
Pages:	1994-2003

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Publication

23229922 | J:336630

First Author:	Gotoh K
Year:	2013
Journal:	Nephrol Dial Transplant
Title:	Obesity-related chronic kidney disease is associated with spleen-derived IL-10.
Volume:	28
Issue:	5
Pages:	1120-30

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Publication

22146087 | J:182778

First Author:	Gotoh K
Year:	2012
Journal:	J Neurochem
Title:	A novel anti-inflammatory role for spleen-derived interleukin-10 in obesity-induced hypothalamic inflammation.
Volume:	120
Issue:	5
Pages:	752-64

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Publication

7860609 | -

First Author:	Carlin A
Year:	1995
Journal:	J Bacteriol
Title:	The ars operon of Escherichia coli confers arsenical and antimonial resistance.
Volume:	177
Issue:	4
Pages:	981-6

•

Publication

9261111 | -

First Author:	Liu J
Year:	1997
Journal:	J Biol Chem
Title:	Ligand interactions of the ArsC arsenate reductase.
Volume:	272
Issue:	34
Pages:	21084-9

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Publication

15028674 | -

First Author:	Zuber P
Year:	2004
Journal:	J Bacteriol
Title:	Spx-RNA polymerase interaction and global transcriptional control during oxidative stress.
Volume:	186
Issue:	7
Pages:	1911-8

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Publication

11004200 | -

First Author:	Borezee E
Year:	2000
Journal:	J Bacteriol
Title:	Identification in Listeria monocytogenes of MecA, a homologue of the Bacillus subtilis competence regulatory protein.
Volume:	182
Issue:	20
Pages:	5931-4

•

Protein Domain

IPR006660 | Arsenate_reductase-like

Type:

Family

Description:

Several bacterial taxon have a chromosomal resistance system, encoded by the ars operon, for the detoxification of arsenate, arsenite, and antimonite []. This system transports arsenite and antimonite out of the cell. The pump is composed of two polypeptides, the products of the arsA and arsB genes. This two-subunit enzyme produces resistance to arsenite and antimonite. Arsenate, however, must first be reduced to arsenite before it is extruded. A third gene, arsC, expands the substrate specificity to allow for arsenate pumping and resistance. ArsC is an approximately 150-residue arsenate reductase that uses reduced glutathione (GSH) to convert arsenate to arsenite with a redox active cysteine residue in the active site. ArsC forms an active quaternary complex with GSH, arsenate, and glutaredoxin 1 (Grx1). The three ligands must be present simultaneously for reduction to occur [].The arsC family also comprises the Spx proteins which are GRAM-positive bacterial transcription factors that regulate the transcription of multiple genes in response to disulphide stress [, ].The arsC protein structure has been solved []. It belongs to the thioredoxin superfamily fold which is defined by a β-sheet core surrounded by α-helices. The active cysteine residue of ArsC is located in the loop between the first β-strand and the first helix, which is also conserved in the Spx protein and its homologues.

•

Protein

E2J863

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX13

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX09

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX05

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX11

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX16

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX15

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX18

Organism:	Mus musculus/domesticus
Length:	214
Fragment?:	true

•

Protein

E3VX10

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX08

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX14

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX17

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX04

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX07

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX03

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX02

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E3VX12

Organism:	Mus musculus/domesticus
Length:	47
Fragment?:	true

•

Protein

E3VX06

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Protein

E2J848

Organism:	Mus musculus/domesticus
Length:	147
Fragment?:	true

•

Protein

E2J849

Organism:	Mus musculus/domesticus
Length:	46
Fragment?:	true

•

Publication

2178921 | -

First Author:	Hardwick KG
Year:	1990
Journal:	EMBO J
Title:	ERD1, a yeast gene required for the retention of luminal endoplasmic reticulum proteins, affects glycoprotein processing in the Golgi apparatus.
Volume:	9
Issue:	3
Pages:	623-30

•

Publication

8412687 | -

First Author:	Kong L
Year:	1993
Journal:	Mol Microbiol
Title:	Sequence and properties of mecA, a negative regulator of genetic competence in Bacillus subtilis.
Volume:	9
Issue:	2
Pages:	365-73

•

Protein Domain

IPR004342 | EXS_C

Type:

Domain

Description:

The EXS domain is named after ERD1/XPR1/SYG1 and proteins containing this motif include the C-terminal of the SYG1 G-protein associated signal transduction protein from Saccharomyces cerevisiae, and sequences that are thought to be Murine leukemia virus (MLV) receptors (XPR1. The N-terminal of these proteins often have an SPX domain () [].While the N-terminal is thought to be involved in signal transduction, the role of the C-terminal is not known. This region of similarity contains several predicted transmembrane helices. This family also includes the ERD1 (ERD: ER retention defective) S. cerevisiae proteins. ERD1 proteins are involved in the localization of endogenous endoplasmic reticulum (ER) proteins. Erd1 null mutants secrete such proteins even though they possess the C-terminal HDEL ER lumen localization label sequence. In addition, null mutants also exhibit defects in the Golgi-dependent processing of several glycoproteins, which led to the suggestion that the sorting of luminal ER proteins actually occurs in the Golgi, with subsequent return of these proteins to the ER via `salvage' vesicles [].

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Protein Domain

IPR008681 | Neg-reg_MecA

Type:

Family

Description:

Competence is the ability of a cell to take up exogenous DNA from its environment, resulting in transformation. It is widespread among bacteria and is probably an important mechanism for the horizontal transfer of genes. DNA usually becomes available by the death and lysis of other cells. Competent bacteria use components of extracellular filaments called type 4 pili to create pores in their membranes and pull DNA through the pores into the cytoplasm. This process, including the development of competence and the expression of the uptake machinery, is regulated in response to cell-cell signalling and/or nutritional conditions [].This family contains several bacterial MecA proteins. In complex media competence development is poor, and there is little or no expression of late competence genes. Overexpression of MecA inhibits comG transcription [, , ].MecA enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. It acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, it inhibits sporulation. It is also involved in Spx degradation by ClpC [].

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Publication

11709171 | -

First Author:	Martin P
Year:	2001
Journal:	Structure
Title:	Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme.
Volume:	9
Issue:	11
Pages:	1071-81

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Publication

8901420 | -

First Author:	Solomon JM
Year:	1996
Journal:	Trends Genet
Title:	Who's competent and when: regulation of natural genetic competence in bacteria.
Volume:	12
Issue:	4
Pages:	150-5

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