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P40136

- CYAA_BACAN

UniProt

P40136 - CYAA_BACAN

Protein

Calmodulin-sensitive adenylate cyclase

Gene

cya

Organism
Bacillus anthracis
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Feb 1995)
      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. 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

    GO - Biological processi

    1. pathogenesis Source: UniProtKB-KW

    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

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi169 – 1691V → A: No effect. 2 Publications
    Mutagenesisi170 – 1701Y → A: Loss of cytotoxicity due to inability to bind PA. 2 Publications
    Mutagenesisi171 – 1711Y → A: Loss of cytotoxicity due to inability to bind PA. 2 Publications
    Mutagenesisi172 – 1721E → A: No effect. 2 Publications
    Mutagenesisi173 – 1731I → A: Loss of cytotoxicity due to inability to bind PA. 2 Publications
    Mutagenesisi174 – 1741G → A: No effect. 2 Publications
    Mutagenesisi175 – 1751K → A: Loss of cytotoxicity due to inability to bind PA. 2 Publications
    Mutagenesisi329 – 3291R → M: Great decrease in activity. 2 Publications
    Mutagenesisi346 – 3461K → M or R: Loss of activity. 3 Publications
    Mutagenesisi346 – 3461K → Q: Loss of activity due to inability to bind the substrate. 3 Publications
    Mutagenesisi353 – 3531K → M, R or A: Loss of activity. 2 Publications
    Mutagenesisi436 – 4361E → Q: Decreases activity. 2 Publications
    Mutagenesisi443 – 4431E → Q: Decreases activity. 2 Publications
    Mutagenesisi491 – 4911D → N: Great decrease in activity. 2 Publications
    Mutagenesisi493 – 4931D → N: Great decrease in activity. 2 Publications
    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 – 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.
    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

    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

    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:
    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...
    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.

    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

    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: October 1, 2014
    This is version 134 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