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P15917

- LEF_BACAN

UniProt

P15917 - LEF_BACAN

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Protein

Lethal factor

Gene

lef

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

Zn2+Note: 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

GO - Biological processi

  1. pathogenesis Source: CACAO
  2. proteolysis Source: CACAO
Complete GO annotation...

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.
ReactomeiREACT_228255. Uptake and function of anthrax toxins.

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MNIKKEFIKV ISMSCLVTAI TLSGPVFIPL VQGAGGHGDV GMHVKEKEKN
60 70 80 90 100
KDENKRKDEE RNKTQEEHLK EIMKHIVKIE VKGEEAVKKE AAEKLLEKVP
110 120 130 140 150
SDVLEMYKAI GGKIYIVDGD ITKHISLEAL SEDKKKIKDI YGKDALLHEH
160 170 180 190 200
YVYAKEGYEP VLVIQSSEDY VENTEKALNV YYEIGKILSR DILSKINQPY
210 220 230 240 250
QKFLDVLNTI KNASDSDGQD LLFTNQLKEH PTDFSVEFLE QNSNEVQEVF
260 270 280 290 300
AKAFAYYIEP QHRDVLQLYA PEAFNYMDKF NEQEINLSLE ELKDQRMLAR
310 320 330 340 350
YEKWEKIKQH YQHWSDSLSE EGRGLLKKLQ IPIEPKKDDI IHSLSQEEKE
360 370 380 390 400
LLKRIQIDSS DFLSTEEKEF LKKLQIDIRD SLSEEEKELL NRIQVDSSNP
410 420 430 440 450
LSEKEKEFLK KLKLDIQPYD INQRLQDTGG LIDSPSINLD VRKQYKRDIQ
460 470 480 490 500
NIDALLHQSI GSTLYNKIYL YENMNINNLT ATLGADLVDS TDNTKINRGI
510 520 530 540 550
FNEFKKNFKY SISSNYMIVD INERPALDNE RLKWRIQLSP DTRAGYLENG
560 570 580 590 600
KLILQRNIGL EIKDVQIIKQ SEKEYIRIDA KVVPKSKIDT KIQEAQLNIN
610 620 630 640 650
QEWNKALGLP KYTKLITFNV HNRYASNIVE SAYLILNEWK NNIQSDLIKK
660 670 680 690 700
VTNYLVDGNG RFVFTDITLP NIAEQYTHQD EIYEQVHSKG LYVPESRSIL
710 720 730 740 750
LHGPSKGVEL RNDSEGFIHE FGHAVDDYAG YLLDKNQSDL VTNSKKFIDI
760 770 780 790 800
FKEEGSNLTS YGRTNEAEFF AEAFRLMHST DHAERLKVQK NAPKTFQFIN

DQIKFIINS
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:
EMBLi
GenBanki
DDBJi
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_001022097.1. NZ_JHDR01000065.1.
WP_010890024.1. NZ_JHCB01000035.1.
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:
EMBLi
GenBanki
DDBJi
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_001022097.1. NZ_JHDR01000065.1.
WP_010890024.1. NZ_JHCB01000035.1.
YP_016503.2. NC_007322.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
Reactomei REACT_228255. Uptake and function of anthrax toxins.

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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 140 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