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P15917

- LEF_BACAN

UniProt

P15917 - LEF_BACAN

Protein

Lethal factor

Gene

lef

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 2 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    One of the three proteins composing the anthrax toxin, the agent which infects many mammalian species and that may cause death. LF is the lethal factor that, when associated with PA, causes death. LF is not toxic by itself. It is a protease that cleaves the N-terminal of most dual specificity mitogen-activated protein kinase kinases (MAPKKs or MAP2Ks) (except for MAP2K5). Cleavage invariably occurs within the N-terminal proline-rich region preceding the kinase domain, thus disrupting a sequence involved in directing specific protein-protein interactions necessary for the assembly of signaling complexes. There may be other cytosolic targets of LF involved in cytotoxicity. The proteasome may mediate a toxic process initiated by LF in the cell cytosol involving degradation of unidentified molecules that are essential for macrophage homeostasis. This is an early step in LeTx intoxication, but it is downstream of the cleavage by LF of MEK1 or other putative substrates.5 Publications

    Catalytic activityi

    Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.

    Cofactori

    Binds 1 zinc ion per subunit.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi719 – 7191Zinc; catalytic
    Active sitei720 – 7201
    Metal bindingi723 – 7231Zinc; catalytic
    Metal bindingi768 – 7681Zinc; catalytic

    GO - Molecular functioni

    1. metal ion binding Source: UniProtKB-KW
    2. metallopeptidase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct

    GO - Biological processi

    1. pathogenesis Source: CACAO
    2. proteolysis Source: CACAO

    Keywords - Molecular functioni

    Hydrolase, Metalloprotease, Protease, Toxin

    Keywords - Biological processi

    Virulence

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    BioCyciANTHRA:GBAA_PXO1_0172-MONOMER.
    BANT261594:GJ7F-5757-MONOMER.

    Protein family/group databases

    MEROPSiM34.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lethal factor (EC:3.4.24.83)
    Short name:
    LF
    Alternative name(s):
    Anthrax lethal toxin endopeptidase component
    Gene namesi
    Name:lef
    Ordered Locus Names:pXO1-107, BXA0172, GBAA_pXO1_0172
    Encoded oniPlasmid pXO10 Publication
    OrganismiBacillus anthracis
    Taxonomic identifieri1392 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
    ProteomesiUP000000594: Plasmid pXO1

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi180 – 1801V → A: No effect on PA-binding ability. 1 Publication
    Mutagenesisi181 – 1811Y → A: Loss of ability to bind to PA. 1 Publication
    Mutagenesisi182 – 1821Y → A: Loss of ability to bind to PA. 1 Publication
    Mutagenesisi183 – 1831E → A: No effect on PA-binding ability. 1 Publication
    Mutagenesisi184 – 1841I → A: Loss of ability to bind to PA. 1 Publication
    Mutagenesisi185 – 1851G → A: No effect on PA-binding ability. 1 Publication
    Mutagenesisi186 – 1861K → A: Loss of ability to bind to PA. 1 Publication
    Mutagenesisi220 – 2201D → A: Loss of ability to bind to PA and loss of toxicity. 1 Publication
    Mutagenesisi221 – 2211L → A: No effect on PA-binding ability and fully toxic. 1 Publication
    Mutagenesisi222 – 2221L → A: No effect on PA-binding ability and fully toxic. 1 Publication
    Mutagenesisi223 – 2231F → A: Loss of ability to bind to PA and non-toxic. 1 Publication
    Mutagenesisi719 – 7191H → A: Loss of activity and zinc binding. 1 Publication
    Mutagenesisi720 – 7201E → C or D: Loss of activity. No effect on zinc binding. 1 Publication
    Mutagenesisi723 – 7231H → A: Loss of activity and zinc binding. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 33331 PublicationAdd
    BLAST
    Chaini34 – 809776Lethal factorPRO_0000029233Add
    BLAST

    Expressioni

    Inductioni

    Positively transcriptionally regulated by AtxA, which, in turn, is induced by bicarbonate and high temperatures (37 degrees Celsius).

    Interactioni

    Subunit structurei

    Anthrax toxins are composed of three distinct proteins, a protective antigen (PA), a lethal factor (LF) and an edema factor (EF). None of these is toxic by itself. PA+LF forms the lethal toxin (LeTx); PA+EF forms the edema toxin (EdTx).3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    pagAP134235EBI-456923,EBI-456868

    Protein-protein interaction databases

    DIPiDIP-29871N.
    IntActiP15917. 1 interaction.
    MINTiMINT-7014731.
    STRINGi261594.GBAA_pXO1_0172.

    Structurei

    Secondary structure

    1
    809
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni62 – 654
    Helixi66 – 7611
    Beta strandi77 – 804
    Helixi87 – 9711
    Helixi101 – 1099
    Beta strandi113 – 1197
    Helixi121 – 1233
    Helixi125 – 1273
    Helixi132 – 1354
    Beta strandi136 – 1383
    Beta strandi144 – 1463
    Helixi147 – 1493
    Beta strandi151 – 1555
    Beta strandi157 – 1593
    Beta strandi161 – 1655
    Turni170 – 1723
    Helixi174 – 19017
    Helixi193 – 1964
    Helixi201 – 21111
    Beta strandi213 – 2164
    Helixi217 – 2226
    Helixi225 – 2284
    Helixi236 – 2405
    Helixi243 – 25816
    Helixi260 – 26910
    Helixi271 – 28212
    Helixi284 – 29310
    Helixi300 – 31011
    Helixi312 – 3176
    Helixi320 – 33011
    Helixi337 – 3426
    Helixi346 – 3549
    Helixi357 – 3593
    Beta strandi361 – 3633
    Helixi365 – 37915
    Helixi384 – 3896
    Beta strandi392 – 3943
    Helixi403 – 41210
    Helixi413 – 4153
    Helixi421 – 4288
    Beta strandi435 – 4373
    Helixi439 – 45517
    Beta strandi458 – 4603
    Helixi461 – 4644
    Turni465 – 4673
    Beta strandi470 – 4745
    Helixi476 – 4783
    Helixi481 – 4844
    Beta strandi486 – 4883
    Helixi498 – 5058
    Beta strandi510 – 5156
    Beta strandi518 – 5225
    Beta strandi532 – 5376
    Beta strandi543 – 5475
    Turni548 – 5503
    Beta strandi551 – 5544
    Beta strandi556 – 57015
    Beta strandi573 – 58311
    Helixi585 – 60723
    Beta strandi616 – 6194
    Helixi625 – 64218
    Helixi645 – 65713
    Beta strandi662 – 6676
    Helixi669 – 6713
    Helixi673 – 6764
    Helixi682 – 6843
    Beta strandi688 – 6936
    Helixi694 – 6963
    Beta strandi698 – 7058
    Turni709 – 7113
    Helixi713 – 73321
    Beta strandi735 – 7373
    Helixi741 – 7433
    Helixi745 – 75410
    Helixi761 – 7633
    Helixi766 – 77712
    Helixi782 – 79110
    Helixi793 – 80715

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J7NX-ray2.30A/B34-809[»]
    1JKYX-ray3.90A34-809[»]
    1PWPX-ray2.90A/B34-809[»]
    1PWQX-ray3.52A/B34-809[»]
    1PWUX-ray2.70A/B34-809[»]
    1PWVX-ray2.85A/B34-809[»]
    1PWWX-ray2.80A/B34-809[»]
    1YQYX-ray2.30A297-809[»]
    1ZXVX-ray2.67A/B34-809[»]
    2L0RNMR-A705-809[»]
    3KWVX-ray3.10C/F34-296[»]
    4DV8X-ray1.63A296-809[»]
    ProteinModelPortaliP15917.
    SMRiP15917. Positions 62-809.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP15917.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati315 – 333191Add
    BLAST
    Repeati342 – 357162Add
    BLAST
    Repeati360 – 378193Add
    BLAST
    Repeati380 – 397184Add
    BLAST
    Repeati399 – 416185Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni34 – 293260PA-binding regionSequence AnalysisAdd
    BLAST
    Regioni60 – 295236I; PA-binding regionSequence AnalysisAdd
    BLAST
    Regioni296 – 33035IIAAdd
    BLAST
    Regioni315 – 4161025 X approximate repeatsAdd
    BLAST
    Regioni336 – 41681IIIAdd
    BLAST
    Regioni420 – 583164IIBAdd
    BLAST
    Regioni585 – 809225IVAdd
    BLAST

    Domaini

    It comprises four domains: domain I binds the membrane-translocating component (PA); domains II, III and IV together create a long deep groove that holds the 16-residue N-terminal tail of MAPKK before cleavage. Domain IV contains the catalytic center.
    The PA-binding region is found in both B.anthracis EF and LF.

    Sequence similaritiesi

    Belongs to the peptidase M34 family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG45846.
    HOGENOMiHOG000034565.
    KOiK08645.
    OMAiRMMARYE.
    OrthoDBiEOG62ZHV6.

    Family and domain databases

    Gene3Di1.10.2030.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProiIPR015239. Anthrax_tox_lethal-fac_cen.
    IPR003541. Anthrax_toxin_lethal/edema.
    IPR014781. Anthrax_toxin_lethal/edema_N/C.
    IPR024079. MetalloPept_cat_dom.
    [Graphical view]
    PfamiPF09156. Anthrax-tox_M. 1 hit.
    PF07737. ATLF. 2 hits.
    [Graphical view]
    PRINTSiPR01392. ANTHRAXTOXNA.
    PROSITEiPS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P15917-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNIKKEFIKV ISMSCLVTAI TLSGPVFIPL VQGAGGHGDV GMHVKEKEKN    50
    KDENKRKDEE RNKTQEEHLK EIMKHIVKIE VKGEEAVKKE AAEKLLEKVP 100
    SDVLEMYKAI GGKIYIVDGD ITKHISLEAL SEDKKKIKDI YGKDALLHEH 150
    YVYAKEGYEP VLVIQSSEDY VENTEKALNV YYEIGKILSR DILSKINQPY 200
    QKFLDVLNTI KNASDSDGQD LLFTNQLKEH PTDFSVEFLE QNSNEVQEVF 250
    AKAFAYYIEP QHRDVLQLYA PEAFNYMDKF NEQEINLSLE ELKDQRMLAR 300
    YEKWEKIKQH YQHWSDSLSE EGRGLLKKLQ IPIEPKKDDI IHSLSQEEKE 350
    LLKRIQIDSS DFLSTEEKEF LKKLQIDIRD SLSEEEKELL NRIQVDSSNP 400
    LSEKEKEFLK KLKLDIQPYD INQRLQDTGG LIDSPSINLD VRKQYKRDIQ 450
    NIDALLHQSI GSTLYNKIYL YENMNINNLT ATLGADLVDS TDNTKINRGI 500
    FNEFKKNFKY SISSNYMIVD INERPALDNE RLKWRIQLSP DTRAGYLENG 550
    KLILQRNIGL EIKDVQIIKQ SEKEYIRIDA KVVPKSKIDT KIQEAQLNIN 600
    QEWNKALGLP KYTKLITFNV HNRYASNIVE SAYLILNEWK NNIQSDLIKK 650
    VTNYLVDGNG RFVFTDITLP NIAEQYTHQD EIYEQVHSKG LYVPESRSIL 700
    LHGPSKGVEL RNDSEGFIHE FGHAVDDYAG YLLDKNQSDL VTNSKKFIDI 750
    FKEEGSNLTS YGRTNEAEFF AEAFRLMHST DHAERLKVQK NAPKTFQFIN 800
    DQIKFIINS 809
    Length:809
    Mass (Da):93,770
    Last modified:July 5, 2004 - v2
    Checksum:i2076B4D7277317EE
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti299 – 2991A → S in strain: Sterne.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29081 Genomic DNA. Translation: AAA79216.1.
    M30210 Genomic DNA. Translation: AAA22569.1.
    AF065404 Genomic DNA. Translation: AAD32411.1.
    AE011190 Genomic DNA. Translation: AAM26117.1.
    AE017336 Genomic DNA. Translation: AAT28913.2.
    AJ413934 Genomic DNA. Translation: CAC93932.1.
    AJ413935 Genomic DNA. Translation: CAC93933.1.
    PIRiJQ0032.
    RefSeqiNP_052803.1. NC_001496.1.
    NP_652928.1. NC_003980.1.
    WP_010890024.1. NC_001496.1.
    YP_016503.2. NC_007322.2.

    Genome annotation databases

    EnsemblBacteriaiAAT28913; AAT28913; GBAA_pXO1_0172.
    GeneIDi1158731.
    2820148.
    3361711.
    KEGGibar:GBAA_pXO1_0172.
    PATRICi24662141. VBIBacAnt106580_0160.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M29081 Genomic DNA. Translation: AAA79216.1 .
    M30210 Genomic DNA. Translation: AAA22569.1 .
    AF065404 Genomic DNA. Translation: AAD32411.1 .
    AE011190 Genomic DNA. Translation: AAM26117.1 .
    AE017336 Genomic DNA. Translation: AAT28913.2 .
    AJ413934 Genomic DNA. Translation: CAC93932.1 .
    AJ413935 Genomic DNA. Translation: CAC93933.1 .
    PIRi JQ0032.
    RefSeqi NP_052803.1. NC_001496.1.
    NP_652928.1. NC_003980.1.
    WP_010890024.1. NC_001496.1.
    YP_016503.2. NC_007322.2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J7N X-ray 2.30 A/B 34-809 [» ]
    1JKY X-ray 3.90 A 34-809 [» ]
    1PWP X-ray 2.90 A/B 34-809 [» ]
    1PWQ X-ray 3.52 A/B 34-809 [» ]
    1PWU X-ray 2.70 A/B 34-809 [» ]
    1PWV X-ray 2.85 A/B 34-809 [» ]
    1PWW X-ray 2.80 A/B 34-809 [» ]
    1YQY X-ray 2.30 A 297-809 [» ]
    1ZXV X-ray 2.67 A/B 34-809 [» ]
    2L0R NMR - A 705-809 [» ]
    3KWV X-ray 3.10 C/F 34-296 [» ]
    4DV8 X-ray 1.63 A 296-809 [» ]
    ProteinModelPortali P15917.
    SMRi P15917. Positions 62-809.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-29871N.
    IntActi P15917. 1 interaction.
    MINTi MINT-7014731.
    STRINGi 261594.GBAA_pXO1_0172.

    Chemistry

    BindingDBi P15917.
    ChEMBLi CHEMBL4372.

    Protein family/group databases

    MEROPSi M34.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAT28913 ; AAT28913 ; GBAA_pXO1_0172 .
    GeneIDi 1158731.
    2820148.
    3361711.
    KEGGi bar:GBAA_pXO1_0172.
    PATRICi 24662141. VBIBacAnt106580_0160.

    Phylogenomic databases

    eggNOGi NOG45846.
    HOGENOMi HOG000034565.
    KOi K08645.
    OMAi RMMARYE.
    OrthoDBi EOG62ZHV6.

    Enzyme and pathway databases

    BioCyci ANTHRA:GBAA_PXO1_0172-MONOMER.
    BANT261594:GJ7F-5757-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P15917.

    Family and domain databases

    Gene3Di 1.10.2030.10. 1 hit.
    3.40.390.10. 2 hits.
    InterProi IPR015239. Anthrax_tox_lethal-fac_cen.
    IPR003541. Anthrax_toxin_lethal/edema.
    IPR014781. Anthrax_toxin_lethal/edema_N/C.
    IPR024079. MetalloPept_cat_dom.
    [Graphical view ]
    Pfami PF09156. Anthrax-tox_M. 1 hit.
    PF07737. ATLF. 2 hits.
    [Graphical view ]
    PRINTSi PR01392. ANTHRAXTOXNA.
    PROSITEi PS00142. ZINC_PROTEASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence and analysis of the lethal factor gene (lef) from Bacillus anthracis."
      Bragg T.S., Robertson D.L.
      Gene 81:45-54(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-49.
    2. "A comparison of Bacillus anthracis sequences."
      Lowe J.
      Submitted (APR-1990) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Sequence and organization of pXO1, the large Bacillus anthracis plasmid harboring the anthrax toxin genes."
      Okinaka R.T., Cloud K., Hampton O., Hoffmaster A.R., Hill K.K., Keim P., Koehler T.M., Lamke G., Kumano S., Mahillon J., Manter D., Martinez Y., Ricke D., Svensson R., Jackson P.J.
      J. Bacteriol. 181:6509-6515(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Sterne.
    4. "Comparative genome sequencing for discovery of novel polymorphisms in Bacillus anthracis."
      Read T.D., Salzberg S.L., Pop M., Shumway M.F., Umayam L., Jiang L., Holtzapple E., Busch J.D., Smith K.L., Schupp J.M., Solomon D., Keim P., Fraser C.M.
      Science 296:2028-2033(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Ames / isolate Florida / A2012.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Ames ancestor.
    6. "Sequence analysis of the genes encoding for the major virulence factors of Bacillus anthracis vaccine strain 'Carbosap'."
      Adone R., Pasquali P., La Rosa G., Marianelli C., Muscillo M., Fasanella A., Francia M., Ciuchini F.
      J. Appl. Microbiol. 93:117-121(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-809.
      Strain: Carbosap and Ferrara.
    7. Cited for: FUNCTION.
    8. "Anthrax lethal factor cleaves the N-terminus of MAPKKs and induces tyrosine/threonine phosphorylation of MAPKs in cultured macrophages."
      Vitale G., Pellizzari R., Recchi C., Napolitani G., Mock M., Montecucco C.
      Biochem. Biophys. Res. Commun. 248:706-711(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    9. "Anthrax lethal factor causes proteolytic inactivation of mitogen-activated protein kinase kinase."
      Duesbery N.S., Vande Woude G.F.
      J. Appl. Microbiol. 87:289-293(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    10. "Susceptibility of mitogen-activated protein kinase kinase family members to proteolysis by anthrax lethal factor."
      Vitale G., Bernardi L., Napolitani G., Mock M., Montecucco C.
      Biochem. J. 352:739-745(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    11. "Proteasome activity is required for anthrax lethal toxin to kill macrophages."
      Tang G., Leppla S.H.
      Infect. Immun. 67:3055-3060(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    12. "Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: a Fourier-transform infrared spectroscopy approach."
      Wang X.-M., Mock M., Ruysschaert J.-M., Cabiaux V.
      Biochemistry 35:14939-14946(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    13. "Zinc content of the Bacillus anthracis lethal factor."
      Kochi S.K., Schiavo G., Mock M., Montecucco C.
      FEMS Microbiol. Lett. 124:343-348(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: ZINC-BINDING.
    14. "The three Bacillus anthracis toxin genes are coordinately regulated by bicarbonate and temperature."
      Sirard J.-C., Mock M., Fouet A.
      J. Bacteriol. 176:5188-5192(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION OF TOXIN EXPRESSION.
      Strain: Sterne.
    15. "Lethal factor active-site mutations affect catalytic activity in vitro."
      Hammond S.E., Hanna P.C.
      Infect. Immun. 66:2374-2378(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF HIS-719; GLU-720 AND HIS-723.
      Strain: Sterne.
    16. "Involvement of residues 147VYYEIGK153 in binding of lethal factor to protective antigen of Bacillus anthracis."
      Gupta P., Singh A., Chauhan V., Bhatnagar R.
      Biochem. Biophys. Res. Commun. 280:158-163(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF VAL-180; TYR-181; TYR-182; GLU-183; ILE-184; GLY-185 AND LYS-186.
      Strain: Sterne.
    17. "Asp 187 and Phe 190 residues in lethal factor are required for the expression of anthrax lethal toxin activity."
      Singh A., Chauhan V., Sodhi A., Bhatnagar R.
      FEMS Microbiol. Lett. 212:183-186(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF ASP-220; LEU-221; LEU-222 AND PHE-223.
      Strain: Sterne.
    18. Cited for: REVIEW.
    19. Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH ZINC IONS AND MAP2K2.
    20. "The structural basis for substrate and inhibitor selectivity of the anthrax lethal factor."
      Turk B.E., Wong T.Y., Schwarzenbacher R., Jarrell E.T., Leppla S.H., Collier R.J., Liddington R.C., Cantley L.C.
      Nat. Struct. Mol. Biol. 11:60-66(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.52 ANGSTROMS) OF 34-809 IN COMPLEX WITH ZINC IONS AND PEPTIDE SUBSTRATE ANALOG.
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 297-809 IN COMPLEX WITH ZINC IONS AND PROTEASE INHIBITOR.

    Entry informationi

    Entry nameiLEF_BACAN
    AccessioniPrimary (citable) accession number: P15917
    Secondary accession number(s): Q8KYJ6, Q933F6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 138 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    LF binds to the heptamer formed by cleaved PA on the host cell membrane. This step is followed by internalization of the hetero-oligomeric complex by receptor-mediated endocytosis. LeTx requires passage through an acidic vesicle for activity; at acidic pH, as the pore is inserted into the membrane, LF is translocated and reaches its cytosolic targets. LF is probably directly involved in its routing, by interacting with the lipid membrane. This interaction could involve a conformational change of LF and/or an oligomerization of the protein. LF may have the capability of partially unfolding in order to cross the membrane.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Plasmid, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3