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P40136

- CYAA_BACAN

UniProt

P40136 - CYAA_BACAN

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Protein
Calmodulin-sensitive adenylate cyclase
Gene
cya, pXO1-122, BXA0141, GBAA_pXO1_0142
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. EF is a calmodulin-dependent adenylyl cyclase that, when associated with PA, causes edema. EF is not toxic by itself and it is required for the survival of germinated spores within macrophages at the early stages of infection. Provokes dramatic elevation of intracellular cAMP levels in the host.

Catalytic activityi

ATP = 3',5'-cyclic AMP + diphosphate.

Cofactori

Calcium.

Enzyme regulationi

It has an absolute requirement for host calmodulin for its activation. Inhibited by ethyl 5-aminopyrazolo[1,5-a]quinazoline-3-carboxylate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei351 – 3511Proton acceptor
Metal bindingi491 – 4911Magnesium
Metal bindingi493 – 4931Magnesium

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. calcium- and calmodulin-responsive adenylate cyclase activity Source: InterPro
  3. metal ion binding Source: UniProtKB-KW
  4. metallopeptidase activity Source: InterPro
  5. protein binding Source: IntAct
Complete GO annotation...

GO - Biological processi

  1. pathogenesis Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Toxin

Keywords - Biological processi

cAMP biosynthesis, Virulence

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciANTHRA:GBAA_PXO1_0142-MONOMER.
BANT261594:GJ7F-5728-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Calmodulin-sensitive adenylate cyclase (EC:4.6.1.1)
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Anthrax edema toxin adenylate cyclase component
Edema factor
Short name:
EF
Gene namesi
Name:cya
Ordered Locus Names:pXO1-122, BXA0141, GBAA_pXO1_0142
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
Mutagenesisi169 – 1691V → A: No effect. 1 Publication
Mutagenesisi170 – 1701Y → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication
Mutagenesisi171 – 1711Y → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication
Mutagenesisi172 – 1721E → A: No effect. 1 Publication
Mutagenesisi173 – 1731I → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication
Mutagenesisi174 – 1741G → A: No effect. 1 Publication
Mutagenesisi175 – 1751K → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication
Mutagenesisi329 – 3291R → M: Great decrease in activity. 1 Publication
Mutagenesisi346 – 3461K → M or R: Loss of activity. 2 Publications
Mutagenesisi346 – 3461K → Q: Loss of activity due to inability to bind the substrate. 2 Publications
Mutagenesisi353 – 3531K → M, R or A: Loss of activity. 1 Publication
Mutagenesisi436 – 4361E → Q: Decreases activity. 1 Publication
Mutagenesisi443 – 4431E → Q: Decreases activity. 1 Publication
Mutagenesisi491 – 4911D → N: Great decrease in activity. 1 Publication
Mutagenesisi493 – 4931D → N: Great decrease in activity. 1 Publication
Mutagenesisi523 – 5231L → A: Little effect on activation by calmodulin.
Mutagenesisi525 – 5251K → A: Great decrease in calmodulin binding.
Mutagenesisi526 – 5261Q → A: Little effect on activation by calmodulin.
Mutagenesisi529 – 5291V → A: Little effect on activation by calmodulin.
Mutagenesisi577 – 5771H → N or D: Loss of function.
Mutagenesisi583 – 5831N → A: Decreases activity.
Mutagenesisi583 – 5831N → Q or H: Loss of function.
Mutagenesisi588 – 5881E → A: Loss of function.
Mutagenesisi590 – 5901D → A: Decreases activity.
Mutagenesisi639 – 6391N → A: Decreases catalysis rate.
Mutagenesisi647 – 6471D → A: Decreases activity due to reduced activation by calmodulin.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 Publication
Add
BLAST
Chaini34 – 800767Calmodulin-sensitive adenylate cyclase
PRO_0000001317Add
BLAST

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). EF probably forms oligomers as part of the translocation machinery, formed by a heterocomplex of PA63 monomers and EF subunits, and it is functional as a monomer in the host cell.

Binary interactionsi

WithEntry#Exp.IntActNotes
calm2P621552EBI-457011,EBI-397568From a different organism.
CALM3P621588EBI-457011,EBI-397435From a different organism.

Protein-protein interaction databases

DIPiDIP-31055N.
IntActiP40136. 3 interactions.
STRINGi261594.GBAA_pXO1_0142.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 693
Helixi76 – 8611
Helixi91 – 999
Beta strandi103 – 1097
Turni111 – 1144
Beta strandi119 – 1224
Beta strandi130 – 1323
Helixi137 – 1393
Beta strandi141 – 1444
Beta strandi147 – 1493
Beta strandi151 – 1555
Turni163 – 1686
Helixi169 – 1768
Turni177 – 1826
Beta strandi183 – 1886
Helixi192 – 1976
Turni198 – 2025
Beta strandi203 – 2064
Turni211 – 2133
Beta strandi215 – 2173
Beta strandi226 – 2294
Turni230 – 2356
Helixi236 – 24914
Beta strandi250 – 2523
Helixi255 – 2595
Beta strandi260 – 2623
Helixi263 – 27311
Helixi275 – 29016
Beta strandi296 – 2983
Helixi299 – 3057
Helixi309 – 32214
Beta strandi324 – 3285
Turni333 – 3353
Helixi336 – 3405
Beta strandi356 – 3605
Beta strandi365 – 3673
Helixi368 – 3703
Turni372 – 3754
Helixi377 – 39317
Turni394 – 3963
Beta strandi397 – 4026
Helixi407 – 4159
Beta strandi424 – 4274
Beta strandi430 – 4367
Beta strandi440 – 45011
Beta strandi452 – 4576
Turni464 – 4663
Beta strandi471 – 4733
Beta strandi475 – 48915
Beta strandi494 – 5007
Helixi501 – 5077
Helixi510 – 5167
Beta strandi517 – 5215
Helixi527 – 5359
Turni536 – 5383
Beta strandi541 – 5433
Beta strandi544 – 5463
Beta strandi547 – 5493
Helixi551 – 56515
Turni566 – 5683
Helixi580 – 5823
Beta strandi593 – 5964
Beta strandi598 – 6003
Beta strandi602 – 6076
Helixi608 – 61811
Helixi620 – 6223
Turni630 – 6334
Beta strandi634 – 6363
Turni637 – 6393
Turni648 – 6503
Turni652 – 6554
Helixi660 – 67415
Beta strandi681 – 6833
Helixi687 – 70620
Helixi707 – 7104
Helixi714 – 73724
Helixi743 – 76725
Helixi771 – 7777
Beta strandi778 – 7803
Helixi786 – 79813

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1K8TX-ray2.60A291-800[»]
1K90X-ray2.75A/B/C291-800[»]
1K93X-ray2.95A/B/C291-800[»]
1LVCX-ray3.60A/B/C291-800[»]
1PK0X-ray3.30A/B/C292-798[»]
1S26X-ray3.00A/B/C291-800[»]
1SK6X-ray3.20A/B/C291-800[»]
1XFUX-ray3.35A/B/C/D/E/F64-800[»]
1XFVX-ray3.35A/B/C/D/E/F33-800[»]
1XFWX-ray3.40A/B/C/D/E/F33-800[»]
1XFXX-ray3.20A/B/C/D/E/F33-800[»]
1XFYX-ray3.30A/B/C/D/E/F33-800[»]
1XFZX-ray3.25A/B/C/D/E/F33-800[»]
1Y0VX-ray3.60A/B/C/D/E/F33-800[»]
DisProtiDP00395.
ProteinModelPortaliP40136.
SMRiP40136. Positions 64-798.

Miscellaneous databases

EvolutionaryTraceiP40136.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 290257Interaction with protective antigen
Add
BLAST
Regioni294 – 34956Catalytic CA1
Add
BLAST
Regioni350 – 489140Catalytic CB
Add
BLAST
Regioni490 – 622133Catalytic CA2
Add
BLAST
Regioni623 – 800178Interaction with calmodulin
Add
BLAST

Domaini

The N-terminal region contains the residues responsible for binding to PA63. The C-terminal region contains the calmodulin-dependent activation domain and the catalytic site. This region is composed of three globular domains: CA, CB and a helical domain connected to CA by a linker. The active site lies at the interface of CA and CB. The metal ion is coordinated by residues from CA; calmodulin probably binds in a multistep fashion first to residues in CA and then to residues present in the linker and the helical domain.1 Publication
The PA-binding region is found in both B.anthracis EF and LF.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG146287.
HOGENOMiHOG000034573.
KOiK11029.
OMAiDKFEVFQ.
OrthoDBiEOG62ZHV6.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR005165. Anthrax_toxin_edema_cen.
IPR003541. Anthrax_toxin_lethal/edema.
IPR014781. Anthrax_toxin_lethal/edema_N/C.
IPR024079. MetalloPept_cat_dom.
[Graphical view]
PfamiPF03497. Anthrax_toxA. 1 hit.
PF07737. ATLF. 1 hit.
[Graphical view]
PRINTSiPR01392. ANTHRAXTOXNA.

Sequencei

Sequence statusi: Complete.

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

P40136-1 [UniParc]FASTAAdd to Basket

« Hide

MTRNKFIPNK FSIISFSVLL FAISSSQAIE VNAMNEHYTE SDIKRNHKTE    50
KNKTEKEKFK DSINNLVKTE FTNETLDKIQ QTQDLLKKIP KDVLEIYSEL 100
GGEIYFTDID LVEHKELQDL SEEEKNSMNS RGEKVPFASR FVFEKKRETP 150
KLIINIKDYA INSEQSKEVY YEIGKGISLD IISKDKSLDP EFLNLIKSLS 200
DDSDSSDLLF SQKFKEKLEL NNKSIDINFI KENLTEFQHA FSLAFSYYFA 250
PDHRTVLELY APDMFEYMNK LEKGGFEKIS ESLKKEGVEK DRIDVLKGEK 300
ALKASGLVPE HADAFKKIAR ELNTYILFRP VNKLATNLIK SGVATKGLNV 350
HGKSSDWGPV AGYIPFDQDL SKKHGQQLAV EKGNLENKKS ITEHEGEIGK 400
IPLKLDHLRI EELKENGIIL KGKKEIDNGK KYYLLESNNQ VYEFRISDEN 450
NEVQYKTKEG KITVLGEKFN WRNIEVMAKN VEGVLKPLTA DYDLFALAPS 500
LTEIKKQIPQ KEWDKVVNTP NSLEKQKGVT NLLIKYGIER KPDSTKGTLS 550
NWQKQMLDRL NEAVKYTGYT GGDVVNHGTE QDNEEFPEKD NEIFIINPEG 600
EFILTKNWEM TGRFIEKNIT GKDYLYYFNR SYNKIAPGNK AYIEWTDPIT 650
KAKINTIPTS AEFIKNLSSI RRSSNVGVYK DSGDKDEFAK KESVKKIAGY 700
LSDYYNSANH IFSQEKKRKI SIFRGIQAYN EIENVLKSKQ IAPEYKNYFQ 750
YLKERITNQV QLLLTHQKSN IEFKLLYKQL NFTENETDNF EVFQKIIDEK 800
Length:800
Mass (Da):92,478
Last modified:February 1, 1995 - v1
Checksum:iF4F7EB485DF4C5A6
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501V → E in AAA79215. 1 Publication
Sequence conflicti510 – 5101Q → T AA sequence 1 Publication
Sequence conflicti512 – 5132EW → RM AA sequence 1 Publication
Sequence conflicti760 – 7601V → L in CAA00652. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23179 Genomic DNA. Translation: AAA22374.1.
M24074 Genomic DNA. Translation: AAA79215.1.
A07289 Unassigned DNA. Translation: CAA00652.1. Sequence problems.
AF065404 Genomic DNA. Translation: AAD32426.1.
AE011190 Genomic DNA. Translation: AAM26089.1.
AE017336 Genomic DNA. Translation: AAT28883.2.
AJ413930 Genomic DNA. Translation: CAC93924.1.
AJ413931 Genomic DNA. Translation: CAC93925.1.
PIRiB59106.
JS0029.
RefSeqiNP_052818.1. NC_001496.1.
NP_652900.1. NC_003980.1.
WP_000197748.1. NC_001496.1.
YP_016473.2. NC_007322.2.

Genome annotation databases

EnsemblBacteriaiAAT28883; AAT28883; GBAA_pXO1_0142.
GeneIDi1158701.
2820138.
3361726.
KEGGibar:GBAA_pXO1_0142.
PATRICi24662079. VBIBacAnt106580_0129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M23179 Genomic DNA. Translation: AAA22374.1 .
M24074 Genomic DNA. Translation: AAA79215.1 .
A07289 Unassigned DNA. Translation: CAA00652.1 . Sequence problems.
AF065404 Genomic DNA. Translation: AAD32426.1 .
AE011190 Genomic DNA. Translation: AAM26089.1 .
AE017336 Genomic DNA. Translation: AAT28883.2 .
AJ413930 Genomic DNA. Translation: CAC93924.1 .
AJ413931 Genomic DNA. Translation: CAC93925.1 .
PIRi B59106.
JS0029.
RefSeqi NP_052818.1. NC_001496.1.
NP_652900.1. NC_003980.1.
WP_000197748.1. NC_001496.1.
YP_016473.2. NC_007322.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1K8T X-ray 2.60 A 291-800 [» ]
1K90 X-ray 2.75 A/B/C 291-800 [» ]
1K93 X-ray 2.95 A/B/C 291-800 [» ]
1LVC X-ray 3.60 A/B/C 291-800 [» ]
1PK0 X-ray 3.30 A/B/C 292-798 [» ]
1S26 X-ray 3.00 A/B/C 291-800 [» ]
1SK6 X-ray 3.20 A/B/C 291-800 [» ]
1XFU X-ray 3.35 A/B/C/D/E/F 64-800 [» ]
1XFV X-ray 3.35 A/B/C/D/E/F 33-800 [» ]
1XFW X-ray 3.40 A/B/C/D/E/F 33-800 [» ]
1XFX X-ray 3.20 A/B/C/D/E/F 33-800 [» ]
1XFY X-ray 3.30 A/B/C/D/E/F 33-800 [» ]
1XFZ X-ray 3.25 A/B/C/D/E/F 33-800 [» ]
1Y0V X-ray 3.60 A/B/C/D/E/F 33-800 [» ]
DisProti DP00395.
ProteinModelPortali P40136.
SMRi P40136. Positions 64-798.
ModBasei Search...

Protein-protein interaction databases

DIPi DIP-31055N.
IntActi P40136. 3 interactions.
STRINGi 261594.GBAA_pXO1_0142.

Chemistry

BindingDBi P40136.
ChEMBLi CHEMBL5396.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAT28883 ; AAT28883 ; GBAA_pXO1_0142 .
GeneIDi 1158701.
2820138.
3361726.
KEGGi bar:GBAA_pXO1_0142.
PATRICi 24662079. VBIBacAnt106580_0129.

Phylogenomic databases

eggNOGi NOG146287.
HOGENOMi HOG000034573.
KOi K11029.
OMAi DKFEVFQ.
OrthoDBi EOG62ZHV6.

Enzyme and pathway databases

BioCyci ANTHRA:GBAA_PXO1_0142-MONOMER.
BANT261594:GJ7F-5728-MONOMER.

Miscellaneous databases

EvolutionaryTracei P40136.

Family and domain databases

Gene3Di 3.40.390.10. 1 hit.
InterProi IPR005165. Anthrax_toxin_edema_cen.
IPR003541. Anthrax_toxin_lethal/edema.
IPR014781. Anthrax_toxin_lethal/edema_N/C.
IPR024079. MetalloPept_cat_dom.
[Graphical view ]
Pfami PF03497. Anthrax_toxA. 1 hit.
PF07737. ATLF. 1 hit.
[Graphical view ]
PRINTSi PR01392. ANTHRAXTOXNA.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Structural homology between virulence-associated bacterial adenylate cyclases."
    Escuyer V., Duflot E., Sezer O., Danchin A., Mock M.
    Gene 71:293-298(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Nucleotide sequence of the Bacillus anthracis edema factor gene (cya): a calmodulin-dependent adenylate cyclase."
    Robertson D.L., Tippetts M.T., Leppla S.H.
    Gene 73:363-371(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 34-48.
  3. "Nucleotide sequences expressing adenylate cyclase from B.anthracis, proteins having the activity of this adenylate cyclase and biological uses."
    Escuyer V., Duflot E., Mock M., Danchin A.
    Patent number EP0366550, 02-MAY-1990
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Molecular cloning and expression of the Bacillus anthracis edema factor toxin gene: a calmodulin-dependent adenylate cyclase."
    Tippetts M.T., Robertson D.L.
    J. Bacteriol. 170:2263-2266(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "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.
  6. "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.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Ames ancestor.
  8. "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 1-783.
    Strain: Carbosap and Ferrara.
  9. "Structure and interaction of PA63 and EF (edema toxin) of Bacillus anthracis with lipid membrane."
    Wang X.-M., Wattiez R., Mock M., Falmagne P., Ruysschaert J.-M., Cabiaux V.
    Biochemistry 36:14906-14913(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Sterne.
  10. "Translocation of Bacillus anthracis lethal and oedema factors across endosome membranes."
    Guidi-Rontani C., Weber-Levy M., Mock M., Cabiaux V.
    Cell. Microbiol. 2:259-264(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: Sterne.
  11. "Characterization of ATP and calmodulin-binding properties of a truncated form of Bacillus anthracis adenylate cyclase."
    Labruyere E., Mock M., Ladant D., Michelson S., Gilles A.-M., Laoide B., Barzu O.
    Biochemistry 29:4922-4928(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF CALMODULIN-BINDING DOMAIN.
  12. "Fate of germinated Bacillus anthracis spores in primary murine macrophages."
    Guidi-Rontani C., Levy M., Ohayon H., Mock M.
    Mol. Microbiol. 42:931-938(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: EFFECT ON SPORE GERMINATION.
    Strain: Sterne.
  13. "Structure-based inhibitor discovery against adenylyl cyclase toxins from pathogenic bacteria that cause anthrax and whooping cough."
    Soelaiman S., Wei B.Q., Bergson P., Lee Y.-S., Shen Y., Mrksich M., Shoichet B.K., Tang W.-J.
    J. Biol. Chem. 278:25990-25997(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INHIBITION BY QUINAZOLINE COMPOUNDS.
  14. "A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis."
    Xia Z., Storm D.R.
    J. Biol. Chem. 265:6517-6520(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-346; LYS-353 AND GLU-436.
    Strain: SRI-1.
  15. "Structural and ligand-binding properties of a truncated form of Bacillus anthracis adenylate cyclase and of a catalytically inactive variant in which glutamine substitutes for lysine-346."
    Labruyere E., Mock M., Surewicz W.K., Mantsch H.H., Rose T., Munier H., Sarfati R.S., Barzu O.
    Biochemistry 30:2619-2624(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF LYS-346.
    Strain: Sterne.
  16. "Purification of anthrax edema factor from Escherichia coli and identification of residues required for binding to anthrax protective antigen."
    Kumar P., Ahuja N., Bhatnagar R.
    Infect. Immun. 69:6532-6536(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-169; TYR-170; TYR-171; GLU-172; ILE-173; GLY-174 AND LYS-175.
  17. "An extended conformation of calmodulin induces interactions between the structural domains of adenylyl cyclase from Bacillus anthracis to promote catalysis."
    Drum C.L., Yan S.-Z., Sarac R., Mabuchi Y., Beckingham K., Bohm A., Grabarek Z., Tang W.-J.
    J. Biol. Chem. 275:36334-36340(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ARG-329; GLU-443; ASP-491 AND ASP-493.
  18. "Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin."
    Drum C.L., Yan S.-Z., Bard J., Shen Y.-Q., Lu D., Soelaiman S., Grabarek Z., Bohm A., Tang W.-J.
    Nature 415:396-402(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS), MUTAGENESIS.
  19. "Phylogeny of adenylyl cyclases."
    Danchin A.
    Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. Cited for: REVIEW.

Entry informationi

Entry nameiCYAA_BACAN
AccessioniPrimary (citable) accession number: P40136
Secondary accession number(s): Q937W4, Q937W5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: September 3, 2014
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

EF 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. EF requires passage through an acidic vesicle for activity. At acidic pH, the pore is inserted into the membrane, allowing translocation of EF, which probably contributes actively to its own insertion into the membrane. EF remains associated to the vesicle membrane after translocation to the cytosol, with the catalytic domains being exposed on the cytoplasmic face.

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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