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    clsB cardiolipin synthase B [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945409, updated on 3-Dec-2024

    Summary

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    Official Symbol
    clsB
    Official Full Name
    cardiolipin synthase B
    Primary source
    ECOCYC:G6406
    Locus tag
    b0789
    See related
    ASAP:ABE-0002692
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0778; ybhO
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    Genomic context

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    Sequence:
    NC_000913.3 (822498..823739, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene Bax1-I family protein YbhL Neighboring gene Bax1-I family protein YbhM Neighboring gene PF03706 family inner membrane protein YbhN Neighboring gene endonuclease/exonuclease/phosphatase domain-containing protein YbhP Neighboring gene inner membrane protein YbhQ Neighboring gene ABC exporter membrane subunit YbhR Neighboring gene ABC exporter membrane subunit YbhS Neighboring gene ABC exporter ATP binding subunit YbhF

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. In Vivo and in Vitro Synthesis of Phosphatidylglycerol by an Escherichia coli Cardiolipin Synthase. Li C, et al. J Biol Chem, 2016 Nov 25. PMID 27760827, Free PMC Article
    2. Cardiolipin synthases of Escherichia coli have phospholipid class specific phospholipase D activity dependent on endogenous and foreign phospholipids. Jeucken A, et al. Biochim Biophys Acta Mol Cell Biol Lipids, 2018 Oct. PMID 29933046
    3. A second Escherichia coli protein with CL synthase activity. Guo D, et al. Biochim Biophys Acta, 2000 Jan 17. PMID 10634942
    4. Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates. Tan BK, et al. Proc Natl Acad Sci U S A, 2012 Oct 9. PMID 22988102, Free PMC Article
    5. Sequences that direct significant levels of frameshifting are frequent in coding regions of Escherichia coli. Gurvich OL, et al. EMBO J, 2003 Nov 3. PMID 14592990, Free PMC Article

    See all (8) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Study demonstrated that ClsB is clearly is to perform headgroup exchange on endogenous phospholipids, as demonstrated for a variety of primary alcohols.
      Title: Cardiolipin synthases of Escherichia coli have phospholipid class specific phospholipase D activity dependent on endogenous and foreign phospholipids.
    2. the expression of E. coli ClsB significantly increased PG and cardiolipin levels, with the growth deficiency of pgsA null strain also being complemented under such conditions. Identification of this alternative mechanism for PG synthesis not only expands our knowledge of bacterial anionic phospholipid biosynthesis
      Title: In Vivo and in Vitro Synthesis of Phosphatidylglycerol by an Escherichia coli Cardiolipin Synthase.
    3. Data indicate that the cardiolipin synthase DeltaclsABC mutant (clsA, clsB(ybhO) and clsC (ymdC))nlacks detectible cardiolipin (CL) regardless of growth phase or growth conditions.
      Title: Discovery of a cardiolipin synthase utilizing phosphatidylethanolamine and phosphatidylglycerol as substrates.
    Submit: New GeneRIF Correction

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables cardiolipin synthase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables cardiolipin synthase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables cardiolipin synthase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphatidyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phospholipase D activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables phosphotransferase activity, for other substituted phosphate groups IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables transferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in cardiolipin biosynthetic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in cardiolipin biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in cardiolipin biosynthetic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in phospholipid biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    is_active_in membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    cardiolipin synthase B
    NP_415310.1

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      822498..823739 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_415310.1 cardiolipin synthase B [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_415310.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A8T6BI63
      Conserved Domains (1) summary
      PRK11263
      Location:2 → 412
      PRK11263; cardiolipin synthase ClsB
    Nucleotide Protein
    Heading Accession and Version

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