MG1655
W3110
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Gene Report : ftsH
PEC Original Annotations
Essentiality
     Class essential
     References (PMID)
Res Microbiol. 1991;142(2-3):279-82.
Structure and function of the ftsH gene in Escherichia coli.
Ogura T, Tomoyasu T, Yuki T, Morimura S, Begg KJ, Donachie WD, Mori H, Niki H, Hiraga S. ( 1925026 )
     Deletion OCL29,30-6 (AK4-11 / BK5-11) (D)  ,  OCL29-6 (D)  
Related gene (W3110 PEC)
     Gene Search Search MG1655 PEC by gene name:  ftsH
Related strains
     Strains Search Search strains by gene name:  ftsH   Search strains by all related name:  ftsH b3178 ECK3167 f644 ftsH hflB JW3145 mrsC std tolZ

General information  (Go to Linear View:)
 Gene Name ftsH  
 Alternative name b3178,ECK3167,f644,ftsH,hflB,JW3145,mrsC,std,tolZ  
 Location, Length 3,323,023 - 3,324,957 (  -  ) ;   71.62 min ; 1935 (bp) ,   644 (aa) Go to Linear View
 Product protease, ATP-dependent zinc-metallo  
 Operon Name rlmE-ftsH  
 Note GO_component: GO:0009274 - peptidoglycan-based cell wall; GO_component: GO:0019866 - organelle inner membrane  
 Function enzyme; Degradation of proteins, peptides, glyco  
 Gene Ontology GO:0000166 ; nucleotide binding ( hflB )
GO:0004222 ; metalloendopeptidase activity ( hflB )
GO:0005515 ; protein binding ( hflB )
GO:0005524 ; ATP binding ( hflB )
GO:0005886 ; plasma membrane ( hflB )
GO:0006508 ; proteolysis ( hflB )
GO:0007049 ; cell cycle ( hflB )
GO:0008233 ; peptidase activity ( hflB )
GO:0008237 ; metallopeptidase activity ( hflB )
GO:0008270 ; zinc ion binding ( hflB )
GO:0016020 ; membrane ( hflB )
GO:0016021 ; integral to membrane ( hflB )
GO:0016787 ; hydrolase activity ( hflB )
GO:0017111 ; nucleoside-triphosphatase activity ( hflB )
GO:0030163 ; protein catabolic process ( hflB )
GO:0046872 ; metal ion binding ( hflB )
GO:0051301 ; cell division ( hflB )
 PID 1789568  
 EC number
  (KEGG Pathway)
 
3.4.24.-  
SWISS-PROT  ( Show simple )
  botton Entry name(Acc.no) FTSH_ECOLI ( P28691 )
    -  Protein name Cell division protein ftsH  
    -  Synonyms EC 3.4.24.-  
    -  Gene name OrderedLocusNames=b3178, SF3218, S3436;  
    -  Comments
  • FUNCTION:Seems to act as an ATP-dependent zinc metallopeptidase. Involved in the degradation of sigma-32. Degrades carboxy-terminal-tagged cytoplasmic proteins. These proteins are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (ssrA) stable RNA.
  • COFACTOR:Binds 1 zinc ion (Potential).
  • SUBCELLULAR LOCATION:Integral membrane protein. Inner membrane.
  • SIMILARITY:In the N-terminal section; belongs to the AAA ATPase family.
  • SIMILARITY:In the C-terminal section; belongs to peptidase family M41.  
  •   botton Entry name(Acc.no) FTSH_ECO57 ( Q8X9L0 )
        -  Protein name Cell division protease ftsH  
        -  Synonyms EC 3.4.24.-  
        -  Gene name Name=hflB; Synonyms=ftsH; OrderedLocusNames=z4540, ECs4057;  
        -  Comments
  • FUNCTION:Seems to act as an ATP-dependent zinc metallopeptidase. Involved in the degradation of sigma-32. Degrades carboxy-terminal-tagged cytoplasmic proteins. These proteins are tagged with an 11-amino-acid nonpolar destabilizing tail via a mechanism involving the 10SA (ssrA) stable RNA (By similarity).
  • COFACTOR:Binds 1 zinc ion (Potential).
  • SUBCELLULAR LOCATION:Integral membrane protein. Inner membrane (By similarity).
  • SIMILARITY:In the N-terminal section; belongs to the AAA ATPase family.
  • SIMILARITY:In the C-terminal section; belongs to peptidase family M41.  

  •  Linear View (Whole Mode)
    View Location
       3310.0  –  3335.0 (KBP)

    Homology Analysis
    BLAST
        Bacteria
             GTOP ftsH (  homologous genes of other bacterias  )  
        PDB     (database updated : 2007.02.20 )
             PSI-BLAST Chain A, Whole Cytosolic Region Of Atp-Dependent Metalloprotease Ftsh (G399l)  
        SWISS-PROT     (database updated : 2007.02.20 )
             BLAST Cell division protease ftsH  
             PSI-BLAST Cell division protease ftsH
        nr     (database updated : 2007.02.20 )
             BLAST ATP-binding protein  
    Pfam 28.0   (database updated : 2015-05 )
        Pfam
    PROSITE
        PROSITE ASN_GLYCOSYLATION    CAMP_PHOSPHO_SITE    PKC_PHOSPHO_SITE    CK2_PHOSPHO_SITE    TYR_PHOSPHO_SITE    MYRISTYL    AMIDATION    ATP_GTP_A    HELIX_LOOP_HELIX    AAA     

    Other Cross-Reference
        COG COG0465O 
        EcoCyc ftsH 

    MMBR References
    J Bacteriol. 1998;180:1920-1928
    The Escherichia coli mrsC gene is required for cell growth and mRNA decay.
    Granger, L. L., E. B. O'Hara, R. F. Wang, F. V. Meffen, K. Armstrong, S. D. Yancey, P. Babitzke, and S. R. Kushner.
    Proc Natl Acad Sci U S A. 1995;92:3516-3520
    Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.
    Herman, C., D. Thevenet, R. D'Ari, and P. Bouloc.
    Proc Natl Acad Sci U S A. 1993;90:10861-10865
    Cell growth and lambda phage development controlled by the same essential Escherichia coli gene, ftsH/hflB.
    Herman, C., T. Ogura, T. Tomoyasu, S. Hiraga, Y. Akiyama, K. Ito, R. Thomas, R. D'Ari, and P. Bouloc.
    J Mol Biol. 1986;187(2):213-24.
    hflB, a new Escherichia coli locus regulating lysogeny and the level of bacteriophage lambda cII protein.
    Banuett F, Hoyt MA, McFarlane L, Echols H, Herskowitz I. ( 2939254 )
    J Bacteriol. 1996;178:3457-3461
    The tolZ gene of Escherichia coli is identified as the ftsH gene.
    Qu, J. N., S. I. Makino, H. Adachi, Y. Koyama, Y. Akiyama, K. Ito, T. Tomoyasu, T. Ogura, and H. Matsuzawa.
    FEBS Lett. 1996;399(1-2):26-8.
    Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli.
    Akiyama Y, Kihara A, Ito K. ( 8980112 )
    J Bacteriol. 1993;175:1344-1351
    The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression.
    Tomoyasu, T., T. Yuki, S. Morimura, H. Mori, K. Yamanaka, H. Niki, S. Hiraga, and T. Ogura.
    J Bacteriol. 1998;180:1929-1938
    Escherichia coli mrsC is an allele of hflB, encoding a membrane-associated ATPase and protease that is required for mRNA decay.
    Wang, R. F., E. B. O'Hara, M. Aldea, C. I. Bargmann, and H. Gromley.

    Sequences
    Amino acid
    FASTA format
    0001 MAKNLILWLV IAVVLMSVFQ SFGPSESNGR KVDYSTFLQE VNNDQVREAR INGREINVTK KDSNRYTTYI 
    0071 PVQDPKLLDN LLTKNVKVVG EPPEEPSLLA SIFISWFPML LLIGVWIFFM RQMQGGGGKG AMSFGKSKAR 
    0141 MLTEDQIKTT FADVAGCDEA KEEVAELVEY LREPSRFQKL GGKIPKGVLM VGPPGTGKTL LAKAIAGEAK 
    0211 VPFFTISGSD FVEMFVGVGA SRVRDMFEQA KKAAPCIIFI DEIDAVGRQR GAGLGGGHDE REQTLNQMLV 
    0281 EMDGFEGNEG IIVIAATNRP DVLDPALLRP GRFDRQVVVG LPDVRGREQI LKVHMRRVPL APDIDAAIIA 
    0351 RGTPGFSGAD LANLVNEAAL FAARGNKRVV SMVEFEKAKD KIMMGAERRS MVMTEAQKES TAYHEAGHAI 
    0421 IGRLVPEHDP VHKVTIIPRG RALGVTFFLP EGDAISASRQ KLESQISTLY GGRLAEEIIY GPEHVSTGAS 
    0491 NDIKVATNLA RNMVTQWGFS EKLGPLLYAE EEGEVFLGRS VAKAKHMSDE TARIIDQEVK ALIERNYNRA 
    0561 RQLLTDNMDI LHAMKDALMK YETIDAPQID DLMARRDVRP PAGWEEPGAS NNSGDNGSPK APRPVDEPRT 
    0631 PNPGNTMSEQ LGDK
    
    
    Nucleotide
    FASTA format

    View sequence out neighbor 100bp
    -100                                             accgggagat ttcagacgaa agtttgaaag 
    -070 atgctggata tagagtatcc tgacgctgtt tttaacacag ttgtaataag aggttaatcc cttgagtgac 
    0001 atggcgaaaa acctaatact ctggctggtc attgccgttg tgctgatgtc agtattccag agctttgggc 
    0071 ccagcgagtc taatggccgt aaggtggatt actctacctt cctacaagag gtcaataacg accaggttcg 
    0141 tgaagcgcgt atcaacggac gtgaaatcaa cgttaccaag aaagatagta accgttatac cacttacatt 
    0211 ccggttcagg atccgaaatt actggataac ctgttgacca agaacgtcaa ggttgtcggt gaaccgcctg 
    0281 aagaaccaag cctgctggct tctatcttca tctcctggtt cccgatgctg ttgctgattg gtgtctggat 
    0351 cttcttcatg cgtcaaatgc agggcggcgg tggcaaaggt gccatgtcgt ttggtaagag caaagcgcgc 
    0421 atgctgacgg aagatcagat caaaacgacc tttgctgacg ttgcgggctg cgacgaagca aaagaagaag 
    0491 ttgctgaact ggttgagtat ctgcgcgagc cgagccgctt ccagaaactc ggcggtaaga tcccgaaagg 
    0561 cgtcttgatg gtcggtcctc cgggtaccgg taaaacgctg ctggcgaaag cgattgcagg cgaagcgaaa 
    0631 gttccgttct ttactatctc cggttctgac ttcgtagaaa tgttcgtcgg tgtgggtgca tcccgtgttc 
    0701 gtgacatgtt cgaacaggcg aagaaagcgg caccgtgcat catctttatc gatgaaatcg acgccgtagg 
    0771 ccgccagcgt ggcgctggtc tgggcggtgg tcacgatgaa cgtgaacaga ctctgaacca gatgctggtt 
    0841 gagatggatg gcttcgaagg taacgaaggt atcatcgtta tcgccgcgac taaccgtccg gacgttctcg 
    0911 acccggccct gctgcgtcct ggccgtttcg accgtcaggt tgtggtcggc ttgccagatg ttcgcggtcg 
    0981 tgagcagatc ctgaaagttc acatgcgtcg cgtaccattg gcacccgata tcgacgcggc aatcattgcc 
    1051 cgtggtactc ctggtttctc cggtgctgac ctggcgaacc tggtgaacga agcggcactg ttcgctgctc 
    1121 gtggcaacaa acgcgttgtg tcgatggttg agttcgagaa agcgaaagac aaaatcatga tgggtgcgga 
    1191 acgtcgctcc atggtgatga cggaagcgca gaaagaatcg acggcttacc acgaagcggg tcatgcgatt 
    1261 atcggtcgcc tggtgccgga acacgatccg gtgcacaaag tgacgattat cccacgcggt cgtgcgctgg 
    1331 gtgtgacttt cttcttgcct gagggcgacg caatcagcgc cagccgtcag aaactggaaa gccagatttc 
    1401 tacgctgtac ggtggtcgtc tggcagaaga gatcatctac gggccggaac atgtatctac cggtgcgtcc 
    1471 aacgatatta aagttgcgac caacctggca cgtaacatgg tgactcagtg gggcttctct gagaaattgg 
    1541 gtccactgct gtacgcggaa gaagaaggtg aagtgttcct cggccgtagc gtagcgaaag cgaaacatat 
    1611 gtccgatgaa actgcacgta tcatcgacca ggaagtgaaa gcactgattg agcgtaacta taatcgtgcg 
    1681 cgtcagcttc tgaccgacaa tatggatatt ctgcatgcga tgaaagatgc tctcatgaaa tatgagacta 
    1751 tcgacgcacc gcagattgat gacctgatgg cacgtcgcga tgtacgtccg ccagcgggct gggaagaacc 
    1821 aggcgcttct aacaattctg gcgacaatgg tagtccaaag gctcctcgtc cggttgatga accgcgtacg 
    1891 ccgaacccgg gtaacaccat gtcagagcag ttaggcgaca agtaagttcc cgcatcagat gactgtattt 
    1961 gtaccgaaaa ccccggggcg tgctccgggg ttttttctta tcaattcata ccagggataa catcatgaaa 
    2031 ctctt