Annotations for this protein have been verified by the authors of the corresponding papers


DP00591: Bifunctional hemolysin/adenylate cyclaseFASTA viewXML view

General information
DisProt:DP00591
Name:Bifunctional hemolysin/adenylate cyclase
Synonym(s):CYAA_BORPE
AC-HLY
Cyclolysin
ACT
Calmodulin-sensitive adenylate cyclase [cleavage product 1]
EC=4.6.1.1
ATP pyrophosphate-lyase
Adenylyl cyclase
Hemolysin [cleavage product 2]
First appeared in release:Release 4.9 (01/06/2009)
UniProt:P15318
UniGene: 
SwissProt: CYAA_BORPE
TrEMBL:  
NCBI (GI): 34978355
Source organism:Bordetella pertussis
Sequence length:1706
Percent disordered:41%
Homologues: 


Native sequence

        10         20         30         40         50         60
         |          |          |          |          |          |
MQQSHQAGYA NAADRESGIP AAVLDGIKAV AKEKNATLMF RLVNPHSTSL IAEGVATKGL - 60
GVHAKSSDWG LQAGYIPVNP NLSKLFGRAP EVIARADNDV NSSLAHGHTA VDLTLSKERL - 120
DYLRQAGLVT GMADGVVASN HAGYEQFEFR VKETSDGRYA VQYRRKGGDD FEAVKVIGNA - 180
AGIPLTADID MFAIMPHLSN FRDSARSSVT SGDSVTDYLA RTRRAASEAT GGLDRERIDL - 240
LWKIARAGAR SAVGTEARRQ FRYDGDMNIG VITDFELEVR NALNRRAHAV GAQDVVQHGT - 300
EQNNPFPEAD EKIFVVSATG ESQMLTRGQL KEYIGQQRGE GYVFYENRAY GVAGKSLFDD - 360
GLGAAPGVPS GRSKFSPDVL ETVPASPGLR RPSLGAVERQ DSGYDSLDGV GSRSFSLGEV - 420
SDMAAVEAAE LEMTRQVLHA GARQDDAEPG VSGASAHWGQ RALQGAQAVA AAQRLVHAIA - 480
LMTQFGRAGS TNTPQEAASL SAAVFGLGEA SSAVAETVSG FFRGSSRWAG GFGVAGGAMA - 540
LGGGIAAAVG AGMSLTDDAP AGQKAAAGAE IALQLTGGTV ELASSIALAL AAARGVTSGL - 600
QVAGASAGAA AGALAAALSP MEIYGLVQQS HYADQLDKLA QESSAYGYEG DALLAQLYRD - 660
KTAAEGAVAG VSAVLSTVGA AVSIAAAASV VGAPVAVVTS LLTGALNGIL RGVQQPIIEK - 720
LANDYARKID ELGGPQAYFE KNLQARHEQL ANSDGLRKML ADLQAGWNAS SVIGVQTTEI - 780
SKSALELAAI TGNADNLKSV DVFVDRFVQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT - 840
FITPLAAPGE EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN - 900
GVLKHSIKLD VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT VSADGERFNV - 960
RKQLNNANVY REGVATQTTA YGKRTENVQY RHVELARVGQ LVEVDTLEHV QHIIGGAGND - 1020
SITGNAHDNF LAGGSGDDRL DGGAGNDTLV GGEGQNTVIG GAGDDVFLQD LGVWSNQLDG - 1080
GAGVDTVKYN VHQPSEERLE RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSR - 1140
LNDRIAGDDQ DNELWGHDGN DTIRGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD - 1200
IDGGAGLDTV DYSAMIHPGR IVAPHEYGFG IEADLSREWV RKASALGVDY YDNVRNVENV - 1260
IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD GNDMLYGDAG NDTLYGGLGD - 1320
DTLEGGAGND WFGQTQAREH DVLRGGDGVD TVDYSQTGAH AGIAAGRIGL GILADLGAGR - 1380
VDKLGEAGSS AYDTVSGIEN VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG - 1440
DGDDQLSGDA GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG RDTVDFSGPG RGLDAGAKGV - 1500
FLSLGKGFAS LMDEPETSNV LRNIENAVGS ARDDVLIGDA GANVLNGLAG NDVLSGGAGD - 1560
DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGVGYGHDT IYESGGGHDT IRINAGADQL - 1620
WFARQGNDLE IRILGTDDAL TVHDWYRDAD HRVEIIHAAN QAVDQAGIEK LVEAMAQYPD - 1680
PGAAAAAPPA ARVPDTLMQS LAVNWR



Functional narrative    

This adenylate cyclase belongs to a special class of bacterial toxin. It causes whooping cough by acting on mammalian cells by elevating cAMP-concentration and thus disrupts normal cell function. The intrinsically disordered region is natively unfolded in the absence of calcium. The toxin is secreted by the Type 1 Secretion System, a narrow channel, prior to eukaryotic cell intoxication. The calcium binding induces the folding of secondary and tertiary structures, together with a strong stabilization and dehydration of the polypeptide.

Region 1: 1006-1706

Map of ordered and disordered regions







Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.


Region 1
Type:Disordered
Name:Repeat in ToXin (RTX)
Location:1006 - 1706
Length:701
Region sequence:

TLEHVQHIIGGAGNDSITGNAHDNFLAGGSGDDRLDGGAGNDTLVGGEGQNTVIGGAGDD
VFLQDLGVWSNQLDGGAGVDTVKYNVHQPSEERLERMGDTGIHADLQKGTVEKWPALNLF
SVDHVKNIENLHGSRLNDRIAGDDQDNELWGHDGNDTIRGRGGDDILRGGLGLDTLYGED
GNDIFLQDDETVSDDIDGGAGLDTVDYSAMIHPGRIVAPHEYGFGIEADLSREWVRKASA
LGVDYYDNVRNVENVIGTSMKDVLIGDAQANTLMGQGGDDTVRGGDGDDLLFGGDGNDML
YGDAGNDTLYGGLGDDTLEGGAGNDWFGQTQAREHDVLRGGDGVDTVDYSQTGAHAGIAA
GRIGLGILADLGAGRVDKLGEAGSSAYDTVSGIENVVGTELADRITGDAQANVLRGAGGA
DVLAGGEGDDVLLGGDGDDQLSGDAGRDRLYGEAGDDWFFQDAANAGNLLDGGDGRDTVD
FSGPGRGLDAGAKGVFLSLGKGFASLMDEPETSNVLRNIENAVGSARDDVLIGDAGANVL
NGLAGNDVLSGGAGDDVLLGDEGSDLLSGDAGNDDLFGGQGDDTYLFGVGYGHDTIYESG
GGHDTIRINAGADQLWFARQGNDLEIRILGTDDALTVHDWYRDADHRVEIIHAANQAVDQ
AGIEKLVEAMAQYPDPGAAAAAPPAARVPDTLMQSLAVNWR

Modification type: Fragment
PDB:  
Structural/functional type: Function arises via a disorder to order transition
Functional classes:  
Functional subclasses: Substrate/ligand binding
Detection methods:
  1. Analytical ultracentrifugation (298 K; ProteomeLab XL-I (analytical ultracentrifuge ); two-channel Epon centerpiece 1.2 mm; wavelength 276 nm)

  2. Circular dichroism (CD) spectroscopy, far-UV (Aviv 215 (spectrometer); bandwidth 1 nm; scan rate 0.5 nm/s)

  3. Circular dichroism (CD) spectroscopy, near-UV (Aviv 215 (spectrometer); bandwidth 1 nm; scan rate 0.5 nm/s)

  4. Fluorescence, intrinsic (bandwidth 5 cm; FP-6200 (spectrofluorimeter); path length (quartz cells ) 1 cm; protein (sample) 2 mL; scan rate 25 nm/min; wavelength 292 nm)
References:
  1. Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. "RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion." J Biol Chem. 2009; 284(3): 1781-9. PubMed: 19015266

  2. Sotomayor Pérez AC, Karst JC, Davi M, Guijarro JI, Ladant D, Chenal A. "Characterization of the regions involved in the calcium-induced folding of the intrinsically disordered RTX motifs from the bordetella pertussis adenylate cyclase toxin." 2010; 397(2): 534-549. PubMed: 20096704
Comments:
 



References

  1. Chenal A, Guijarro JI, Raynal B, Delepierre M, Ladant D. "RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion." J. Biol. Chem.. 2008; 284(3): 1781-9. PubMed: 19015266

  2. Szilvay GR, Blenner MA, Shur O, Cropek DM, Banta S. "A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordetella pertussis adenylate cyclase." Biochemistry. 2009; 48(47): 11273-82. PubMed: 19860484



Comments


The disordered region lies within the residues corresponding to hemolysin (cleavage product 2)(residues 313-1706). A separate entry for hemolysin will be needed.


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