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    hypF carbamoyl--[HypE] ligase [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 944963, updated on 3-Dec-2024

    Summary

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    Official Symbol
    hypF
    Official Full Name
    carbamoyl--[HypE] ligase
    Primary source
    ECOCYC:EG11551
    Locus tag
    b2712
    See related
    ASAP:ABE-0008915
    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
    ECK2707; hydA
    Summary
    FhlA regulon. [More information is available at EcoGene: EG11551]. NiFe-hydrogenases have one CO and two CN groups bound as ligands to the iron. [More information is available at EcoCyc: EG11551].
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    Genomic context

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    Sequence:
    NC_000913.3 (2835173..2837425, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene D-arabinose 5-phosphate isomerase GutQ Neighboring gene DNA-binding transcriptional dual regulator NorR Neighboring gene anaerobic nitric oxide reductase flavorubredoxin Neighboring gene NADH:flavorubredoxin reductase Neighboring gene putative electron transport protein HydN Neighboring gene DNA-binding transcriptional repressor AscG

    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. Investigating the effects of mutations on protein aggregation in the cell. Calloni G, et al. J Biol Chem, 2005 Mar 18. PMID 15611128
    2. Genetic analysis of mutants of Escherichia coli K12 and Salmonella typhimurium LT2 deficient in hydrogenase activity. Pascal MC, et al. Mol Gen Genet, 1975 Nov 24. PMID 1107810
    3. Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from the HypF N-terminal domain. Chiti F, et al. Protein Sci, 2001 Dec. PMID 11714922, Free PMC Article
    4. Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF. Rosano C, et al. Acta Crystallogr D Biol Crystallogr, 2002 Mar. PMID 11856843
    5. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases. Bucciantini M, et al. Nature, 2002 Apr 4. PMID 11932737

    See all (36) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.
      Title: Toxic oligomers of the amyloidogenic HypF-N protein form pores in mitochondrial membranes.
    2. These findings demonstrate that it is possible to isolate incompletely processed intermediates on the maturation pathway and to use these to activate apo-forms of [NiFe]-hydrogenase large subunits.
      Title: [NiFe]-hydrogenase maturation in vitro: analysis of the roles of the HybG and HypD accessory proteins1.
    3. Data support model in which HypB-SlyD complex establishes communication between GTP hydrolysis and nickel delivery and provide insight into role of HypB-SlyD complex during [NiFe]-hydrogenase biosynthesis.
      Title: Escherichia coli SlyD, more than a Ni(II) reservoir.
    4. structural flexibility of HypF-N protein and hydrophobic exposure are primary determinants of the ability of oligomeric assemblies to cause cellular dysfunction and its consequences, such as neurodegeneration.
      Title: A causative link between the structure of aberrant protein oligomers and their toxicity.
    5. Experiments reveal that HypF and HypE associate to form a stoichiometric, hetero-oligomeric complex predominantly consisting of a [EF]2 heterotetramer which exists in a dynamic equilibrium with the EF heterodimer.
      Title: Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF.
    6. Data indicate that HypF-N is capable of forming amyloid protofibrils and fibrils under conditions in which the protein is initially in a predominantly native-like conformation.
      Title: Amyloid formation from HypF-N under conditions in which the protein is initially in its native state.
    Submit: New GeneRIF Correction

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables carboxyl- or carbamoyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables carboxyl- or carbamoyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables carboxyl- or carbamoyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables double-stranded RNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in protein maturation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein maturation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein maturation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in protein-containing complex assembly IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of ATPase complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    carbamoyl--[HypE] ligase

    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
      2835173..2837425 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417192.1 carbamoyl--[HypE] ligase [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417192.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A2X1M5L7
      Conserved Domains (2) summary
      TIGR00143
      Location:42 → 739
      hypF; [NiFe] hydrogenase maturation protein HypF
      cl00551
      Location:9 → 48
      Acylphosphatase
    Nucleotide Protein
    Heading Accession and Version

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