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BACAN:CYAA

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Species (Taxon ID) Bacillus anthracis. (1392)
Gene Name(s) cya
Protein Name(s) Calmodulin-sensitive adenylate cyclase

ATP pyrophosphate-lyase Adenylyl cyclase Anthrax edema toxin adenylate cyclase component Edema factor EF

External Links
UniProt P40136
EMBL M23179
M24074
A07289
AF065404
AE011190
AE017336
AJ413930
AJ413931
PIR B59106
JS0029
RefSeq NP_052818.1
NP_652900.1
WP_000197748.1
YP_016473.2
PDB 1K8T
1K90
1K93
1LVC
1PK0
1S26
1SK6
1XFU
1XFV
1XFW
1XFX
1XFY
1XFZ
1Y0V
PDBsum 1K8T
1K90
1K93
1LVC
1PK0
1S26
1SK6
1XFU
1XFV
1XFW
1XFX
1XFY
1XFZ
1Y0V
DisProt DP00395
ProteinModelPortal P40136
SMR P40136
DIP DIP-31055N
IntAct P40136
STRING 261594.GBAA_pXO1_0142
BindingDB P40136
ChEMBL CHEMBL5396
EnsemblBacteria AAT28883
GeneID 1158701
2820138
3361726
KEGG bar:GBAA_pXO1_0142
PATRIC 24662079
eggNOG NOG146287
HOGENOM HOG000034573
KO K11029
OMA DKFEVFQ
OrthoDB EOG62ZHV6
BioCyc ANTHRA:GBAA_PXO1_0142-MONOMER
BANT261594:GJ7F-5728-MONOMER
Reactome REACT_228255
EvolutionaryTrace P40136
Proteomes UP000000594
GO GO:0005576
GO:0005524
GO:0008294
GO:0046872
GO:0008237
GO:0009405
Gene3D 3.40.390.10
InterPro IPR005165
IPR003541
IPR014781
IPR024079
Pfam PF03497
PF07737
PRINTS PR01392

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0008294

calcium- and calmodulin-responsive adenylate cyclase activity

PMID:2108958[1]

ECO:0000314

F

Table 1: Adenylyl cyclase activity corrected for the amount of recombinant protein expressed.

complete
CACAO 10499

GO:0008237

metallopeptidase activity

PMID:2108958[1]

ECO:0000314

F

See section 'Activation of EF3 by Mutant Forms of CaM', which discusses the activity of protein mutants that have some of the four standard Ca2+ altered.

complete
CACAO 10512

GO:0008294

calcium- and calmodulin-responsive adenylate cyclase activity

PMID:1900429[2]

ECO:0000314

F

See section 'Calmodulin-Binding Properties of CYA 62 K346Q', as well as Figure 6. The next section 'Nucleotide-Binding Properties of CYA 62 K346Q' discusses CYA 62 activity in response to Calcium ion concentration.

complete
CACAO 10513

GO:0008237

metallopeptidase activity

PMID:1900429[2]

ECO:0000314

F

See section 'Nucleotide-Binding Properties of CYA 62 K346Q', which discusses how CYA-62 binding of peptides (3'-dATP, in this case) is regulated by Calcium ion concentration.

complete
CACAO 10514

GO:0044743

intracellular protein transmembrane import

PMID:9398214[3]

ECO:0000314

P

See 'Effect of pH upon PA63, EF, CYA30, and CYA62 Association to Liposomes', and Figure 2. EF (and the two mutant forms CYA30 and CYA62) are the adenylate cyclase protein. An experiment was performed to determine how their affinity for cell wall components is dependent on pH.

complete
CACAO 10533

GO:0044743

intracellular protein transmembrane import

PMID:11207582[4]

ECO:0000314

P

See section 'EF remained associated with endosomal membrane after translocation', Figure 2(B), and Figure 4. Unlike LF, EF crosses the cell membrane enough to expose its active sites to the interior of the cell, but does not fully escape into the interior.

complete
CACAO 10534

enables

GO:0005516

calmodulin binding

PMID:11807546[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0DP25

F

Seeded From UniProt

complete

enables

GO:0005516

calmodulin binding

PMID:11807546[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0DP24

F

Seeded From UniProt

complete

enables

GO:0005516

calmodulin binding

PMID:11807546[5]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:P0DP23

F

Seeded From UniProt

complete

part_of

GO:1902494

catalytic complex

PMID:11807546[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0099004

calmodulin dependent kinase signaling pathway

PMID:11807546[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0008294

calcium- and calmodulin-responsive adenylate cyclase activity

PMID:11807546[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

PMID:11807546[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

PMID:11807546[5]

ECO:0000315

mutant phenotype evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0008294

calcium- and calmodulin-responsive adenylate cyclase activity

PMID:2108958[1]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0004016

adenylate cyclase activity

PMID:6285339[6]

ECO:0000269

experimental evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0006508

proteolysis

GO_REF:0000108

ECO:0000366

evidence based on logical inference from automatic annotation used in automatic assertion

GO:0008237

P

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541
InterPro:IPR005165
InterPro:IPR037017

C

Seeded From UniProt

complete

enables

GO:0008237

metallopeptidase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR024079

F

Seeded From UniProt

complete

enables

GO:0008294

calcium- and calmodulin-responsive adenylate cyclase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR005165
InterPro:IPR037017

F

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541
InterPro:IPR005165
InterPro:IPR037017

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003541

F

Seeded From UniProt

complete

enables

GO:0004016

adenylate cyclase activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.6.1.1

F

Seeded From UniProt

complete

involved_in

GO:0052007

biosynthesis by symbiont of substance in host

Reactome:R-HSA-5211224

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006171

cAMP biosynthetic process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0115

P

Seeded From UniProt

complete

involved_in

GO:0009405

pathogenesis

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0843

P

Seeded From UniProt

complete

enables

GO:0046872

metal ion binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0479

F

Seeded From UniProt

complete

part_of

GO:0005576

extracellular region

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0964
UniProtKB-SubCell:SL-0243

C

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0005524

ATP binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0067

F

Seeded From UniProt

complete

enables

GO:0090729

toxin activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0800

F

Seeded From UniProt

complete

enables

GO:0000166

nucleotide binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0547

F

Seeded From UniProt

complete

enables

GO:0005516

calmodulin binding

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0112

F

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ 1.0 1.1 1.2 Xia, ZG & Storm, DR (1990) A-type ATP binding consensus sequences are critical for the catalytic activity of the calmodulin-sensitive adenylyl cyclase from Bacillus anthracis. J. Biol. Chem. 265 6517-20 PubMed GONUTS page
  2. ↑ 2.0 2.1 Labruyère, E et al. (1991) 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. Biochemistry 30 2619-24 PubMed GONUTS page
  3. ↑ Wang, XM et al. (1997) Structure and interaction of PA63 and EF (edema toxin) of Bacillus anthracis with lipid membrane. Biochemistry 36 14906-13 PubMed GONUTS page
  4. ↑ Guidi-Rontani, C et al. (2000) Translocation of Bacillus anthracis lethal and oedema factors across endosome membranes. Cell. Microbiol. 2 259-64 PubMed GONUTS page
  5. ↑ 5.0 5.1 5.2 5.3 5.4 5.5 5.6 5.7 Drum, CL et al. (2002) Structural basis for the activation of anthrax adenylyl cyclase exotoxin by calmodulin. Nature 415 396-402 PubMed GONUTS page
  6. ↑ Leppla, SH (1982) Anthrax toxin edema factor: a bacterial adenylate cyclase that increases cyclic AMP concentrations of eukaryotic cells. Proc. Natl. Acad. Sci. U.S.A. 79 3162-6 PubMed GONUTS page
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