Q57506 · CYAA_BORBR
- ProteinBifunctional hemolysin/adenylate cyclase
- Genecya
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1706 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Bifunctional adenylate cyclase toxin-hemolysin that plays a crucial role in host colonization. It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function.
Calmodulin-sensitive adenylate cyclase
Adenylate cyclase that is activated by host intracellular calmodulin and catalyzes un-regulated conversion of ATP to cAMP, thereby impairing microbicidal functions of immune effector cells and inducing apoptosis of lung macrophages.
Hemolysin
Hemolysin that forms small cation-selective membrane channels, leading to hemolytic activity (By similarity).
The hemolytic activity of CyaA is weak compared with that of the HlyA of E.coli (By similarity).
The hemolytic activity of CyaA is weak compared with that of the HlyA of E.coli (By similarity).
Catalytic activity
Calmodulin-sensitive adenylate cyclase
ATP = 3',5'-cyclic AMP + diphosphate
Activity regulation
Calmodulin-sensitive adenylate cyclase
Activated by host calmodulin.
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | host cell plasma membrane | |
Cellular Component | membrane | |
Molecular Function | ATP binding | |
Molecular Function | calcium ion binding | |
Molecular Function | calcium- and calmodulin-responsive adenylate cyclase activity | |
Molecular Function | calmodulin binding | |
Molecular Function | channel activity | |
Molecular Function | toxin activity | |
Biological Process | cAMP biosynthetic process | |
Biological Process | killing of cells of another organism |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameBifunctional hemolysin/adenylate cyclase
- Alternative names
- Cleaved into 2 chains
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Bordetella
Accessions
- Primary accessionQ57506
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Hemolysin
Host cell membrane ; Multi-pass membrane protein
Keywords
- Cellular component
Phenotypes & Variants
Keywords
- Disease
PTM/Processing
Features
Showing features for chain, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000001318 | 1-312 | Calmodulin-sensitive adenylate cyclase | |||
Sequence: MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEK | ||||||
Chain | PRO_0000001319 | 313-1706 | Hemolysin | |||
Sequence: IFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPGGRSKSSPDVLETVPASPGLRRPSLGAVERQDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSADVFVDRFIQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLEVIGGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQKTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGAGDDRLDGGAGNDTLVGGEGHNTVVGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSSLNDSIAGDDRDNELWGDDGNDTIHGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHAGKIVAPHEYGFGIEADLSEGWVRKAARRGMDYYDSVRSVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTPAREHDVLRGGAGVDTVDYSQAGAHAGVATGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGNDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRHIENAVGSVRDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGAGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEAIHAANQAIDPAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR | ||||||
Lipidation | 860 | N6-palmitoyl lysine | ||||
Sequence: K | ||||||
Lipidation | 983 | N6-palmitoyl lysine | ||||
Sequence: K |
Post-translational modification
Released in a processed form.
Hemolysin
Palmitoylated at Lys-860 and Lys-983 by CyaC. The toxin only becomes active when modified in position Lys-983: palmitoylation is required for efficient membrane insertion and pore formation of the acylated Hemolysin chain.
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for region, repeat.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-399 | A, catalytic | ||||
Sequence: MQQSHQAGYANAADRESGIPAAVLDGIKAVAKEKNATLMFRLVNPHSTSLIAEGVATKGLGVHAKSSDWGLQAGYIPVNPNLSKLFGRAPEVIARADNDVNSSLAHGHTAVDLTLSKERLDYLRQAGLVTGMADGVVASNHAGYEQFEFRVKETSDGRYAVQYRRKGGDDFEAVKVIGNAAGIPLTADIDMFAIMPHLSNFRDSARSSVTSGDSVTDYLARTRRAASEATGGLDRERIDLLWKIARAGARSAVGTEARRQFRYDGDMNIGVITDFELEVRNALNRRAHAVGAQDVVQHGTEQNNPFPEADEKIFVVSATGESQMLTRGQLKEYIGQQRGEGYVFYENRAYGVAGKSLFDDGLGAAPGVPGGRSKSSPDVLETVPASPGLRRPSLGAVER | ||||||
Region | 367-405 | Disordered | ||||
Sequence: GVPGGRSKSSPDVLETVPASPGLRRPSLGAVERQDSGYD | ||||||
Region | 400-912 | B, Ala/Gly-rich | ||||
Sequence: QDSGYDSLDGVGSRSFSLGEVSDMAAVEAAELEMTRQVLHAGARQDDAEPGVSGASAHWGQRALQGAQAVAAAQRLVHAIALMTQFGRAGSTNTPQEAASLSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVVTSLLTGALNGILRGVQQPIIEKLANDYARKIDELGGPQAYFEKNLQARHEQLANSDGLRKMLADLQAGWNASSVIGVQTTEISKSALELAAITGNADNLKSADVFVDRFIQGERVAGQPVVLDVAAGGIDIASRKGERPALTFITPLAAPGEEQRRRTKTGKSEFTTFVEIVGKQDRWRIRDGAADTTIDLAKVVSQLVDANGVLKHSIKLEVI | ||||||
Region | 500-698 | Required for interaction with CyaC | ||||
Sequence: LSAAVFGLGEASSAVAETVSGFFRGSSRWAGGFGVAGGAMALGGGIAAAVGAGMSLTDDAPAGQKAAAGAEIALQLTGGTVELASSIALALAAARGVTSGLQVAGASAGAAAGALAAALSPMEIYGLVQQSHYADQLDKLAQESSAYGYEGDALLAQLYRDKTAAEGAVAGVSAVLSTVGAAVSIAAAASVVGAPVAVV | ||||||
Region | 913-1656 | C | ||||
Sequence: GGDGDDVVLANASRIHYDGGAGTNTVSYAALGRQDSITVSADGERFNVRKQLNNANVYREGVATQKTAYGKRTENVQYRHVELARVGQLVEVDTLEHVQHIIGGAGNDSITGNAHDNFLAGGAGDDRLDGGAGNDTLVGGEGHNTVVGGAGDDVFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLFSVDHVKNIENLHGSSLNDSIAGDDRDNELWGDDGNDTIHGRGGDDILRGGLGLDTLYGEDGNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHAGKIVAPHEYGFGIEADLSEGWVRKAARRGMDYYDSVRSVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDMLYGDAGNDTLYGGLGDDTLEGGAGNDWFGQTPAREHDVLRGGAGVDTVDYSQAGAHAGVATGRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGADVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGNDTVDFSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRHIENAVGSVRDDVLIGDAGANVLNGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGAGYGHDTIYESGGGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEAI | ||||||
Repeat | 1014-1031 | Hemolysin-type calcium-binding 1 | ||||
Sequence: IGGAGNDSITGNAHDNFL | ||||||
Repeat | 1032-1049 | Hemolysin-type calcium-binding 2 | ||||
Sequence: AGGAGDDRLDGGAGNDTL | ||||||
Repeat | 1050-1067 | Hemolysin-type calcium-binding 3 | ||||
Sequence: VGGEGHNTVVGGAGDDVF | ||||||
Repeat | 1155-1172 | Hemolysin-type calcium-binding 4 | ||||
Sequence: WGDDGNDTIHGRGGDDIL | ||||||
Repeat | 1173-1190 | Hemolysin-type calcium-binding 5 | ||||
Sequence: RGGLGLDTLYGEDGNDIF | ||||||
Repeat | 1279-1296 | Hemolysin-type calcium-binding 6 | ||||
Sequence: MGQGGDDTVRGGDGDDLL | ||||||
Repeat | 1297-1314 | Hemolysin-type calcium-binding 7 | ||||
Sequence: FGGDGNDMLYGDAGNDTL | ||||||
Repeat | 1315-1332 | Hemolysin-type calcium-binding 8 | ||||
Sequence: YGGLGDDTLEGGAGNDWF | ||||||
Repeat | 1335-1352 | Hemolysin-type calcium-binding 9 | ||||
Sequence: TPAREHDVLRGGAGVDTV | ||||||
Repeat | 1411-1428 | Hemolysin-type calcium-binding 10 | ||||
Sequence: TGDAQANVLRGAGGADVL | ||||||
Repeat | 1429-1446 | Hemolysin-type calcium-binding 11 | ||||
Sequence: AGGEGDDVLLGGDGDDQL | ||||||
Repeat | 1447-1464 | Hemolysin-type calcium-binding 12 | ||||
Sequence: SGDAGRDRLYGEAGDDWF | ||||||
Repeat | 1468-1484 | Hemolysin-type calcium-binding 13 | ||||
Sequence: AANAGNLLDGGDGNDTV | ||||||
Repeat | 1537-1554 | Hemolysin-type calcium-binding 14 | ||||
Sequence: IGDAGANVLNGLAGNDVL | ||||||
Repeat | 1555-1572 | Hemolysin-type calcium-binding 15 | ||||
Sequence: SGGAGDDVLLGDEGSDLL | ||||||
Repeat | 1573-1590 | Hemolysin-type calcium-binding 16 | ||||
Sequence: SGDAGNDDLFGGQGDDTY | ||||||
Repeat | 1603-1620 | Hemolysin-type calcium-binding 17 | ||||
Sequence: ESGGGHDTIRINAGADQL | ||||||
Region | 1657-1706 | D, Asp/Gly-rich | ||||
Sequence: HAANQAIDPAGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR |
Domain
The Gly-rich region is probably involved in binding calcium, which is required for target cell-binding or cytolytic activity.
Sequence similarities
In the N-terminal section; belongs to the adenylyl cyclase class-2 family.
In the C-terminal section; belongs to the RTX prokaryotic toxin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length1,706
- Mass (Da)177,056
- Last updated2003-09-19 v4
- ChecksumAF51E8270EA8A68F
Sequence caution
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 292 | in Ref. 1; CAA85481 | ||||
Sequence: A → R | ||||||
Sequence conflict | 371 | in Ref. 1; CAA85481 | ||||
Sequence: G → R | ||||||
Sequence conflict | 546-547 | in Ref. 1; CAA85481 | ||||
Sequence: AA → G |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
Z37112 EMBL· GenBank· DDBJ | CAA85481.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
BX640437 EMBL· GenBank· DDBJ | CAE30822.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |