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    ftsH ATP-dependent zinc metalloprotease FtsH [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 947690, updated on 3-Dec-2024

    Summary

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    Official Symbol
    ftsH
    Official Full Name
    ATP-dependent zinc metalloprotease FtsH
    Primary source
    ECOCYC:EG11506
    Locus tag
    b3178
    See related
    ASAP:ABE-0010444
    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
    ECK3167; hflB; mrsC; std; tolZ
    Summary
    HtpX collaborates with FtsH to eliminate abnormal membrane proteins: an hflX ftsH double mutant is temperature sensitive for growth. [More information is available at EcoGene: EG11506]. FtsH is a membrane-bound, ATP-dependent metalloprotease which has been shown to be involved in the degradation of some aberrant membrane and cytoplasmic proteins . [More information is available at EcoCyc: EG11506].
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    Genomic context

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    Sequence:
    NC_000913.3 (3325001..3326935, complement)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene Sec translocon subunit SecG Neighboring gene phosphoglucosamine mutase Neighboring gene dihydropteroate synthase Neighboring gene 23S rRNA 2'-O-ribose U2552 methyltransferase Neighboring gene ribosome assembly factor YhbY

    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. Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB). Akiyama Y, et al. EMBO J, 2000 Aug 1. PMID 10921871, Free PMC Article
    2. Polypeptide binding of Escherichia coli FtsH (HflB). Akiyama Y, et al. Mol Microbiol, 1998 May. PMID 9643547
    3. Roles of the periplasmic domain of Escherichia coli FtsH (HflB) in protein interactions and activity modulation. Akiyama Y, et al. J Biol Chem, 1998 Aug 28. PMID 9712851
    4. Regulation of bacteriophage lambda development by guanosine 5'-diphosphate-3'-diphosphate. Slomińska M, et al. Virology, 1999 Sep 30. PMID 10502521
    5. Second transmembrane segment of FtsH plays a role in its proteolytic activity and homo-oligomerization. Makino S, et al. FEBS Lett, 1999 Nov 5. PMID 10556534

    See all (122) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. YejM Modulates Activity of the YciM/FtsH Protease Complex To Prevent Lethal Accumulation of Lipopolysaccharide.
      Title: YejM Modulates Activity of the YciM/FtsH Protease Complex To Prevent Lethal Accumulation of Lipopolysaccharide.
    2. Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186.
      Title: Instability of CII is needed for efficient switching between lytic and lysogenic development in bacteriophage 186.
    3. The increased synthesis of sigma(32) is accompanied by stabilization of sigma(32), which is normally very unstable and rapidly degraded by the membrane-localized FtsH protease. It was recently found that sigma(32) must be localized to the inner membrane by the SRP-dependent pathway to work properly for regulation, but the roles played by membrane and other components of the cell remained unknown.
      Title: Regulation of the heat shock response in Escherichia coli: history and perspectives.
    4. FtsH-mediated coordination of lipopolysaccharide biosynthesis correlates with the growth rate.
      Title: FtsH-mediated coordination of lipopolysaccharide biosynthesis in Escherichia coli correlates with the growth rate and the alarmone (p)ppGpp.
    5. FtsH degraded the phage shock protein C in Escherichia coli.
      Title: FtsH-dependent degradation of phage shock protein C in Yersinia enterocolitica and Escherichia coli.
    6. FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm.
      Title: FtsH-dependent processing of RNase colicins D and E3 means that only the cytotoxic domains are imported into the cytoplasm.
    7. report the first purification of E. coli HflK and HflC separately as active and functional proteins and show that each can interact with HflB on its own and each inhibits the proteolysis of lambdaCII
      Title: Escherichia coli HflK and HflC can individually inhibit the HflB (FtsH)-mediated proteolysis of lambdaCII in vitro.
    8. RpoH fragment composed of residues 37-147 is degraded in an FtsH-dependent manner.
      Title: Region C of the Escherichia coli heat shock sigma factor RpoH (sigma 32) contains a turnover element for proteolysis by the FtsH protease.
    9. Data show that FtsH regulates the concentration of the lipid moiety of LPS (lipid A) as well as the sugar moiety (KDO-based core oligosaccharides), ensuring a balanced synthesis of LPS.
      Title: Dual role of FtsH in regulating lipopolysaccharide biosynthesis in Escherichia coli.
    10. inhibition of HflB-mediated proteolysis of sigma(32) by CIII is very similar to that of lambdaCII, characterized by an enhanced protection by the core CIII peptide CIIIC (amino acids 14-41 of lambdaCIII) & lack of interaction between sigma(32) & CIII.
      Title: Direct CIII-HflB interaction is responsible for the inhibition of the HflB (FtsH)-mediated proteolysis of Escherichia coli sigma(32) by lambdaCIII.
    Submit: New GeneRIF Correction See all GeneRIFs (16)

    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 ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP binding ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    enables ATP hydrolysis activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables ATP-dependent peptidase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ATP-dependent peptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ATP-dependent peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metalloendopeptidase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metalloendopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metallopeptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables peptidase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables zinc ion binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables zinc ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables zinc ion binding ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in protein catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in protein catabolic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proteolysis EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in proteolysis IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within proteolysis IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in proteolysis IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within proteolysis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of membrane protein complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    is_active_in plasma membrane IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in plasma membrane IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane ISM
    Inferred from Sequence Model
    more info
    		 PubMed 
    part_of plasma membrane protein complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ATP-dependent zinc metalloprotease FtsH

    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
      3325001..3326935 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_417645.1 ATP-dependent zinc metalloprotease FtsH [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_417645.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9ANQ9
      Conserved Domains (1) summary
      PRK10733
      Location:1 → 644
      hflB; ATP-dependent zinc metalloprotease FtsH
    Nucleotide Protein
    Heading Accession and Version

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