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P15917

- LEF_BACAN

UniProt

P15917 - LEF_BACAN

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Protein

Lethal factor

Gene
lef, pXO1-107, BXA0172, GBAA_pXO1_0172
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

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
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.

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
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).1 Publication

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).

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.

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 region Reviewed predictionAdd
BLAST
Regioni60 – 295236I; PA-binding region Reviewed predictionAdd
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.

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

« 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: September 3, 2014
This is version 137 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

Similar proteinsi