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P40136

- CYAA_BACAN

UniProt

P40136 - CYAA_BACAN

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Protein

Calmodulin-sensitive adenylate cyclase

Gene

cya

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

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

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.
ReactomeiREACT_228255. Uptake and function of anthrax toxins.

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-KW
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. 1 Publication
Mutagenesisi525 – 5251K → A: Great decrease in calmodulin binding. 1 Publication
Mutagenesisi526 – 5261Q → A: Little effect on activation by calmodulin. 1 Publication
Mutagenesisi529 – 5291V → A: Little effect on activation by calmodulin. 1 Publication
Mutagenesisi577 – 5771H → N or D: Loss of function. 1 Publication
Mutagenesisi583 – 5831N → A: Decreases activity. 1 Publication
Mutagenesisi583 – 5831N → Q or H: Loss of function. 1 Publication
Mutagenesisi588 – 5881E → A: Loss of function. 1 Publication
Mutagenesisi590 – 5901D → A: Decreases activity. 1 Publication
Mutagenesisi639 – 6391N → A: Decreases catalysis rate. 1 Publication
Mutagenesisi647 – 6471D → A: Decreases activity due to reduced activation by calmodulin. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 33331 PublicationAdd
BLAST
Chaini34 – 800767Calmodulin-sensitive adenylate cyclasePRO_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

1
800
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi67 – 693Combined sources
Helixi76 – 8611Combined sources
Helixi91 – 999Combined sources
Beta strandi103 – 1097Combined sources
Turni111 – 1144Combined sources
Beta strandi119 – 1224Combined sources
Beta strandi130 – 1323Combined sources
Helixi137 – 1393Combined sources
Beta strandi141 – 1444Combined sources
Beta strandi147 – 1493Combined sources
Beta strandi151 – 1555Combined sources
Turni163 – 1686Combined sources
Helixi169 – 1768Combined sources
Turni177 – 1826Combined sources
Beta strandi183 – 1886Combined sources
Helixi192 – 1976Combined sources
Turni198 – 2025Combined sources
Beta strandi203 – 2064Combined sources
Turni211 – 2133Combined sources
Beta strandi215 – 2173Combined sources
Beta strandi226 – 2294Combined sources
Turni230 – 2356Combined sources
Helixi236 – 24914Combined sources
Beta strandi250 – 2523Combined sources
Helixi255 – 2595Combined sources
Beta strandi260 – 2623Combined sources
Helixi263 – 27311Combined sources
Helixi275 – 29016Combined sources
Beta strandi296 – 2983Combined sources
Helixi299 – 3057Combined sources
Helixi309 – 32214Combined sources
Beta strandi324 – 3285Combined sources
Turni333 – 3353Combined sources
Helixi336 – 3405Combined sources
Beta strandi356 – 3605Combined sources
Beta strandi365 – 3673Combined sources
Helixi368 – 3703Combined sources
Turni372 – 3754Combined sources
Helixi377 – 39317Combined sources
Turni394 – 3963Combined sources
Beta strandi397 – 4026Combined sources
Helixi407 – 4159Combined sources
Beta strandi424 – 4274Combined sources
Beta strandi430 – 4367Combined sources
Beta strandi440 – 45011Combined sources
Beta strandi452 – 4576Combined sources
Turni464 – 4663Combined sources
Beta strandi471 – 4733Combined sources
Beta strandi475 – 48915Combined sources
Beta strandi494 – 5007Combined sources
Helixi501 – 5077Combined sources
Helixi510 – 5167Combined sources
Beta strandi517 – 5215Combined sources
Helixi527 – 5359Combined sources
Turni536 – 5383Combined sources
Beta strandi541 – 5433Combined sources
Beta strandi544 – 5463Combined sources
Beta strandi547 – 5493Combined sources
Helixi551 – 56515Combined sources
Turni566 – 5683Combined sources
Helixi580 – 5823Combined sources
Beta strandi593 – 5964Combined sources
Beta strandi598 – 6003Combined sources
Beta strandi602 – 6076Combined sources
Helixi608 – 61811Combined sources
Helixi620 – 6223Combined sources
Turni630 – 6334Combined sources
Beta strandi634 – 6363Combined sources
Turni637 – 6393Combined sources
Turni648 – 6503Combined sources
Turni652 – 6554Combined sources
Helixi660 – 67415Combined sources
Beta strandi681 – 6833Combined sources
Helixi687 – 70620Combined sources
Helixi707 – 7104Combined sources
Helixi714 – 73724Combined sources
Helixi743 – 76725Combined sources
Helixi771 – 7777Combined sources
Beta strandi778 – 7803Combined sources
Helixi786 – 79813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP40136.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 290257Interaction with protective antigenAdd
BLAST
Regioni294 – 34956Catalytic CA1Add
BLAST
Regioni350 – 489140Catalytic CBAdd
BLAST
Regioni490 – 622133Catalytic CA2Add
BLAST
Regioni623 – 800178Interaction with calmodulinAdd
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.
The PA-binding region is found in both B.anthracis EF and LF.

Sequence similaritiesi

Belongs to the adenylyl cyclase class-2 family.Curated

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

        10         20         30         40         50
MTRNKFIPNK FSIISFSVLL FAISSSQAIE VNAMNEHYTE SDIKRNHKTE
60 70 80 90 100
KNKTEKEKFK DSINNLVKTE FTNETLDKIQ QTQDLLKKIP KDVLEIYSEL
110 120 130 140 150
GGEIYFTDID LVEHKELQDL SEEEKNSMNS RGEKVPFASR FVFEKKRETP
160 170 180 190 200
KLIINIKDYA INSEQSKEVY YEIGKGISLD IISKDKSLDP EFLNLIKSLS
210 220 230 240 250
DDSDSSDLLF SQKFKEKLEL NNKSIDINFI KENLTEFQHA FSLAFSYYFA
260 270 280 290 300
PDHRTVLELY APDMFEYMNK LEKGGFEKIS ESLKKEGVEK DRIDVLKGEK
310 320 330 340 350
ALKASGLVPE HADAFKKIAR ELNTYILFRP VNKLATNLIK SGVATKGLNV
360 370 380 390 400
HGKSSDWGPV AGYIPFDQDL SKKHGQQLAV EKGNLENKKS ITEHEGEIGK
410 420 430 440 450
IPLKLDHLRI EELKENGIIL KGKKEIDNGK KYYLLESNNQ VYEFRISDEN
460 470 480 490 500
NEVQYKTKEG KITVLGEKFN WRNIEVMAKN VEGVLKPLTA DYDLFALAPS
510 520 530 540 550
LTEIKKQIPQ KEWDKVVNTP NSLEKQKGVT NLLIKYGIER KPDSTKGTLS
560 570 580 590 600
NWQKQMLDRL NEAVKYTGYT GGDVVNHGTE QDNEEFPEKD NEIFIINPEG
610 620 630 640 650
EFILTKNWEM TGRFIEKNIT GKDYLYYFNR SYNKIAPGNK AYIEWTDPIT
660 670 680 690 700
KAKINTIPTS AEFIKNLSSI RRSSNVGVYK DSGDKDEFAK KESVKKIAGY
710 720 730 740 750
LSDYYNSANH IFSQEKKRKI SIFRGIQAYN EIENVLKSKQ IAPEYKNYFQ
760 770 780 790 800
YLKERITNQV QLLLTHQKSN IEFKLLYKQL NFTENETDNF EVFQKIIDEK
Length:800
Mass (Da):92,478
Last modified:February 1, 1995 - v1
Checksum:iF4F7EB485DF4C5A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti350 – 3501V → E in AAA79215. (PubMed:3149607)Curated
Sequence conflicti510 – 5101Q → T AA sequence (PubMed:3149607)Curated
Sequence conflicti512 – 5132EW → RM AA sequence (PubMed:3149607)Curated
Sequence conflicti760 – 7601V → L in CAA00652. 1 PublicationCurated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. NZ_JHDR01000048.1.
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:
EMBLi
GenBanki
DDBJi
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. NZ_JHDR01000048.1.
YP_016473.2. NC_007322.2.

3D structure databases

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

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: November 26, 2014
This is version 136 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