sat

sat
168

sulfate adenylyltransferase

Locus
BSU_15590
Molecular weight
42.73 kDa
Isoelectric point
5.65
Protein length
382 aaSequenceBlast
Gene length
1149 bpSequenceBlast
Function
sulfate activation
Product
sulfate adenylyltransferase
Essential
no
E.C.
2.7.7.4
Synonyms
sat, ylnB
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG2046 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,632,208 1,633,356
The protein
Catalyzed reaction/ biological activity
ATP + H+ + sulfate --> adenosine 5'-phosphosulfate + diphosphate (according to UniProt)
Protein family
sulfate adenylyltransferase family (with YitA, according to UniProt)
Structure
1V47 (PDB) (from Thermus thermophilus, 42% identity) PubMed
O34764 (AlphaFold)
Paralogous protein(s)
YitA
Additional information
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Genes
cysH-cysP-sat-cysC-ylnD-sirB-ylnF
Description
PubMed
Regulation
induced by methionine starvation (S-box) PubMed
the S-box RNA is degraded by RNase Y PubMed
Regulatory mechanism
CymR: transcription repression, [pubmed|], in cymR regulon
S-box: RNA switch, , the S-box riboswitch binds S-adenosylmethionine resulting in termination PubMed, in S-box
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
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cysH→ylnF

2025-03-26 23:14:36

Jstuelk

129

ee26ed9bec04d4ffdc2deea174a197c7290dfe30

AC610BA23AE4EE98F22EC54E46509E3060BAE285

Biological materials
Mutant
GP4476 (trpC2 Δsat::neo), available in Jörg Stülke's lab
MGNA-B366 (ylnB::erm), available at the NBRP B. subtilis, Japan
BKE15590 (sat::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATAATATCCATCTCCTCCT, downstream forward: _UP4_GGCGTATCTTAAGGAGGACT
BKK15590 (sat::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATAATATCCATCTCCTCCT, downstream forward: _UP4_GGCGTATCTTAAGGAGGACT
Labs working on this gene/protein
[[Isabelle Martin-Verstraete]], Institute Pasteur, Paris, France
References
Tomsic J, McDaniel BA, Grundy FJ, Henkin TM Natural variability in S-adenosylmethionine (SAM)-dependent riboswitches: S-box elements in bacillus subtilis exhibit differential sensitivity to SAM In vivo and in vitro. Journal of bacteriology. 2008 Feb; 190(3):823-33. . PMID:18039762
Albanesi D, Mansilla MC, Schujman GE, de Mendoza D Bacillus subtilis cysteine synthetase is a global regulator of the expression of genes involved in sulfur assimilation. Journal of bacteriology. 2005 Nov; 187(22):7631-8. . PMID:16267287
Eymann C, Dreisbach A, Albrecht D, Bernhardt J, Becher D, Gentner S, Tam le T, Büttner K, Buurman G, Scharf C, Venz S, Völker U, Hecker M A comprehensive proteome map of growing Bacillus subtilis cells. Proteomics. 2004 Oct; 4(10):2849-76. . PMID:15378759
Taguchi Y, Sugishima M, Fukuyama K Crystal structure of a novel zinc-binding ATP sulfurylase from Thermus thermophilus HB8. Biochemistry. 2004 Apr 13; 43(14):4111-8. . PMID:15065853
Mäder U, Homuth G, Scharf C, Büttner K, Bode R, Hecker M Transcriptome and proteome analysis of Bacillus subtilis gene expression modulated by amino acid availability. Journal of bacteriology. 2002 Aug; 184(15):4288-95. . PMID:12107147
Mansilla MC, Albanesi D, de Mendoza D Transcriptional control of the sulfur-regulated cysH operon, containing genes involved in L-cysteine biosynthesis in Bacillus subtilis. Journal of bacteriology. 2000 Oct; 182(20):5885-92. . PMID:11004190

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Time of last update: 2025-04-10 03:58:59

Author of last update: Robert.warneke