citB

citB
168

aconitase, trigger enzyme

Locus
BSU_18000
Molecular weight
99.14 kDa
Isoelectric point
4.9
Protein length
909 aaSequenceBlast
Gene length
2730 bpSequenceBlast
Function
TCA cycle
Product
aconitase, trigger enzyme
Essential
no
E.C.
4.2.1.3
Synonyms
citB
Outlinks
BsubCyc SubtiList UniProt STRING Genoscapist PaperBLAST

Genomic Context

Categories containing this gene/protein

List of homologs in different organisms, belongs to COG1048 (Galperin et al., 2021)

This gene is a member of the following regulons

Gene
Coordinates
1,926,680 1,929,409
Phenotypes of a mutant
glutamate auxotrophy and a defect in sporulation PubMed
The protein
Catalyzed reaction/ biological activity
Citrate --> isocitrate (according to UniProt)
3-hydroxybutane-1,2,3-tricarboxylate --> 2-methyl-cis-aconitate + H2O (according to UniProt)
Binding to iron responsive elements (IRE RNA) in the absence of the FeS cluster PubMed
2-methylaconitate --> 2-methyl-isocitrate in the methylcitric acid cycle PubMed
Protein family
aconitase/IPM isomerase family (with LeuC, according to UniProt)
Cofactors
FeS cluster PubMed
Structure
2B3X (PDB) (the human enzyme, 53% identity) PubMed
P09339 (AlphaFold)
Additional information
CitB is degraded in the forespore using MdfA as the adaptor protein PubMed
B. subtilis aconitase is both an enzyme and an RNA binding protein (moonlighting protein) PubMed
extensive information on the structure and enzymatic properties of CitB can be found at Proteopedia
belongs to the 100 most abundant proteins PubMed
Expression and Regulation
Operons
Genes
citB-yneN
Description
PubMed
Regulation
expressed upon transition into the stationary phase (AbrB) PubMed, indirect negative regulation by AbrB PubMed
Regulatory mechanism
CodY: repression, PubMed, in codY regulon
CcpC: repression, (molecular inducer: citrate) PubMed PubMed, in ccpC regulon
CcpA: repression, PubMed, in ccpA regulon
Sigma factors
SigA: sigma factor, PubMed, in sigA regulon
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citB→yneN

2025-04-04 08:12:20

ghost

166

11c3575e19719d9d98495e9324e23aee6d346029

4D8AE4853A402B931A1A3D2C11A2983642117BB6

Other regulations
FsrA: translation repression, PubMed
Biological materials
Mutant
GP1275 (citB::erm), available in Jörg Stülke's lab
GP1441 (citB::spec), available in Jörg Stülke's lab
1A999 (citB::spec), PubMed, available at BGSC
GP2338 (citB::kan, Cre-recombinase is integrated in sacA), available in Jörg Stülke's lab
GP2339 (citB::lox72, Cre-recombinase is integrated in sacA), available in Jörg Stülke's lab
BKE18000 (citB::erm trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTCTCCAAAATCCCCCTT, downstream forward: _UP4_TGATGAATCAATAGGAAGAG
BKK18000 (citB::kan trpC2) available at BGSC, PubMed, upstream reverse: _UP1_CATTCTCCAAAATCCCCCTT, downstream forward: _UP4_TGATGAATCAATAGGAAGAG
Expression vectors
pFM1, expression of CitB with a cleavable His6-tag at the C-terminus in E. coli, based on pBAD30, available in Jörg Stülke's lab PubMed
pGP939, expression in E. coli, based on pBluescript, available in Jörg Stülke's lab
pGP1810, expression of Strep-CitB in E. coli, based on pGP172, available in Jörg Stülke's lab
Two-hybrid system
B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Jörg Stülke's lab
FLAG-tag construct
GP1144 citB-3xFLAG spc (based on pGP1331), available in Jörg Stülke's lab
GP1145 citB-3xFLAG kan, available in Jörg Stülke's lab
LacZ fusion
pGP700 (cat, based on pAC5]), available in Jörg Stülke's lab
Antibody
available in Linc Sonenshein's lab
GFP fusion
GP1434 (spc, based on pGP1870), available in Jörg Stülke's lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
References
Reviews
Ul Haq I, Müller P, Brantl SIntermolecular Communication in Bacillus subtilis: RNA-RNA, RNA-Protein and Small Protein-Protein Interactions.Frontiers in molecular biosciences. 2020; 7:178. PMID: 32850966
Volz K The functional duality of iron regulatory protein 1. Current opinion in structural biology. 2008 Feb; 18(1):106-11. doi:10.1016/j.sbi.2007.12.010. PMID:18261896
Commichau FM, Stülke J Trigger enzymes: bifunctional proteins active in metabolism and in controlling gene expression. Molecular microbiology. 2008 Feb; 67(4):692-702. . PMID:18086213
Kiley PJ, Beinert H The role of Fe-S proteins in sensing and regulation in bacteria. Current opinion in microbiology. 2003 Apr; 6(2):181-5. . PMID:12732309
Switzer RL Non-redox roles for iron-sulfur clusters in enzymes. BioFactors (Oxford, England). 1989 Dec; 2(2):77-86. . PMID:2696478
Original Publications
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Time of last update: 2025-04-06 12:17:09

Author of last update: Jstuelk