Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Calmodulin-sensitive adenylate cyclase

Gene

cya

Organism
Bacillus anthracis
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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.

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.

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei351Proton acceptor1
<p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi491Magnesium1
Metal bindingi493Magnesium1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • adenylate cyclase activity Source: Reactome
  • ATP binding Source: CAFA
  • calcium- and calmodulin-responsive adenylate cyclase activity Source: CACAO
  • calmodulin binding Source: CAFA
  • metal ion binding Source: CAFA
  • metallopeptidase activity Source: InterPro
  • toxin activity Source: UniProtKB-KW

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionCalmodulin-binding, Lyase, Toxin
Biological processcAMP biosynthesis, Virulence
LigandATP-binding, Calcium, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-5210891 Uptake and function of anthrax toxins

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:cya
Ordered Locus Names:pXO1-122, BXA0141, GBAA_pXO1_0142
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates if the gene coding for the protein originates from the hydrogenosome, the mitochondrion, the nucleomorph, different plastids or a plasmid. The absence of this section means that the gene is located in one of the main chromosomal element(s).<p><a href='/help/encoded_on' target='_top'>More...</a></p>Encoded oniPlasmid pXO10 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiBacillus anthracis
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri1392 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000594 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Plasmid pXO1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Secreted

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi169V → A: No effect. 1 Publication1
Mutagenesisi170Y → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication1
Mutagenesisi171Y → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication1
Mutagenesisi172E → A: No effect. 1 Publication1
Mutagenesisi173I → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication1
Mutagenesisi174G → A: No effect. 1 Publication1
Mutagenesisi175K → A: Loss of cytotoxicity due to inability to bind PA. 1 Publication1
Mutagenesisi329R → M: Great decrease in activity. 1 Publication1
Mutagenesisi346K → M or R: Loss of activity. 2 Publications1
Mutagenesisi346K → Q: Loss of activity due to inability to bind the substrate. 2 Publications1
Mutagenesisi353K → M, R or A: Loss of activity. 1 Publication1
Mutagenesisi436E → Q: Decreases activity. 1 Publication1
Mutagenesisi443E → Q: Decreases activity. 1 Publication1
Mutagenesisi491D → N: Great decrease in activity. 1 Publication1
Mutagenesisi493D → N: Great decrease in activity. 1 Publication1
Mutagenesisi523L → A: Little effect on activation by calmodulin. 1 Publication1
Mutagenesisi525K → A: Great decrease in calmodulin binding. 1 Publication1
Mutagenesisi526Q → A: Little effect on activation by calmodulin. 1 Publication1
Mutagenesisi529V → A: Little effect on activation by calmodulin. 1 Publication1
Mutagenesisi577H → N or D: Loss of function. 1 Publication1
Mutagenesisi583N → A: Decreases activity. 1 Publication1
Mutagenesisi583N → Q or H: Loss of function. 1 Publication1
Mutagenesisi588E → A: Loss of function. 1 Publication1
Mutagenesisi590D → A: Decreases activity. 1 Publication1
Mutagenesisi639N → A: Decreases catalysis rate. 1 Publication1
Mutagenesisi647D → A: Decreases activity due to reduced activation by calmodulin. 1 Publication1

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5396

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 331 PublicationAdd BLAST33
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000131734 – 800Calmodulin-sensitive adenylate cyclaseAdd BLAST767

Proteomic databases

PRoteomics IDEntifications database

More...
PRIDEi
P40136

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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.

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

Database of interacting proteins

More...
DIPi
DIP-31055N

Protein interaction database and analysis system

More...
IntActi
P40136, 3 interactors

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P40136

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1800
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Database of protein disorder

More...
DisProti
DP00395

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P40136

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P40136

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P40136

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni34 – 290Interaction with protective antigenAdd BLAST257
Regioni294 – 349Catalytic CA1Add BLAST56
Regioni350 – 489Catalytic CBAdd BLAST140
Regioni490 – 622Catalytic CA2Add BLAST133
Regioni623 – 800Interaction with calmodulinAdd BLAST178

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the adenylyl cyclase class-2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000034573

KEGG Orthology (KO)

More...
KOi
K11029

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
3.40.390.10, 1 hit
3.90.1760.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR035099 Anthrax_toxin_C-terminal
IPR005165 Anthrax_toxin_edema_cen
IPR037017 Anthrax_toxin_edema_cen_sf
IPR003541 Anthrax_toxin_lethal/edema
IPR014781 Anthrax_toxin_lethal/edema_N/C
IPR024079 MetalloPept_cat_dom_sf

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF03497 Anthrax_toxA, 1 hit
PF07737 ATLF, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR01392 ANTHRAXTOXNA

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF81298 SSF81298, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF4F7EB485DF4C5A6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti350V → E in AAA79215 (PubMed:3149607).Curated1
Sequence conflicti510Q → T AA sequence (PubMed:3149607).Curated1
Sequence conflicti512 – 513EW → RM AA sequence (PubMed:3149607).Curated2
Sequence conflicti760V → L in CAA00652 (Ref. 3) Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

Protein sequence database of the Protein Information Resource

More...
PIRi
B59106
JS0029

NCBI Reference Sequences

More...
RefSeqi
NP_052818.1, NC_001496.1
WP_000197748.1, NZ_QPKQ01000017.1

Genome annotation databases

Ensembl bacterial and archaeal genome annotation project

More...
EnsemblBacteriai
AAM26089; AAM26089; BX_A0142
AAT28883; AAT28883; GBAA_pXO1_0142

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
3361726

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
bar:GBAA_pXO1_0142

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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
PIRiB59106
JS0029
RefSeqiNP_052818.1, NC_001496.1
WP_000197748.1, NZ_QPKQ01000017.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB 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
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-31055N
IntActiP40136, 3 interactors

Chemistry databases

BindingDBiP40136
ChEMBLiCHEMBL5396

Proteomic databases

PRIDEiP40136

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM26089; AAM26089; BX_A0142
AAT28883; AAT28883; GBAA_pXO1_0142
GeneIDi3361726
KEGGibar:GBAA_pXO1_0142

Phylogenomic databases

HOGENOMiHOG000034573
KOiK11029

Enzyme and pathway databases

ReactomeiR-HSA-5210891 Uptake and function of anthrax toxins

Miscellaneous databases

EvolutionaryTraceiP40136

Protein Ontology

More...
PROi
PR:P40136

Family and domain databases

Gene3Di3.40.390.10, 1 hit
3.90.1760.10, 1 hit
InterProiView protein in InterPro
IPR035099 Anthrax_toxin_C-terminal
IPR005165 Anthrax_toxin_edema_cen
IPR037017 Anthrax_toxin_edema_cen_sf
IPR003541 Anthrax_toxin_lethal/edema
IPR014781 Anthrax_toxin_lethal/edema_N/C
IPR024079 MetalloPept_cat_dom_sf
PfamiView protein in Pfam
PF03497 Anthrax_toxA, 1 hit
PF07737 ATLF, 1 hit
PRINTSiPR01392 ANTHRAXTOXNA
SUPFAMiSSF81298 SSF81298, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCYAA_BACAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P40136
Secondary accession number(s): Q937W4, Q937W5
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: December 5, 2018
This is version 171 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again