Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q57506 (CYAA_BORBR)

Last modified June 16, 2009. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein namesRecommended name:
    Bifunctional hemolysin/adenylate cyclase
Alternative name(s):
    AC-HLY
    Cyclolysin
    ACT
Cleaved into the following 2 chains:
    1- Recommended name:
            Calmodulin-sensitive adenylate cyclase
              EC=4.6.1.1
        Alternative name(s):
            ATP pyrophosphate-lyase
            Adenylyl cyclase
    2- Recommended name:
            Hemolysin
Gene names
Name: cya
Synonyms: cyaA
Ordered Locus Names: BB0324
OrganismBordetella bronchiseptica (Alcaligenes bronchisepticus) [Complete proteome] [HAMAP]
Taxonomic identifier518 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Hide | Top

Protein attributes

Sequence length1706 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

Hide | Top

General annotation (Comments)

Function

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.

Catalytic activity

ATP = 3',5'-cyclic AMP + diphosphate.

Enzyme regulation

Activated by host calmodulin.

Subcellular location

Secreted.

Domain

The Gly-rich region is probably involved in binding calcium, which is required for target cell-binding or cytolytic activity By similarity.

Post-translational modification

Released in a processed form.

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.

Contains 17 hemolysin-type calcium-binding repeats.

Hide | Top

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Calmodulin-sensitive adenylate cyclase
PRO_0000001318
Chain313 – 17061394Hemolysin Potential
PRO_0000001319

Regions

Repeat1014 – 103118Hemolysin-type calcium-binding 1
Repeat1032 – 104918Hemolysin-type calcium-binding 2
Repeat1050 – 106718Hemolysin-type calcium-binding 3
Repeat1155 – 117218Hemolysin-type calcium-binding 4
Repeat1173 – 119018Hemolysin-type calcium-binding 5
Repeat1279 – 129618Hemolysin-type calcium-binding 6
Repeat1297 – 131418Hemolysin-type calcium-binding 7
Repeat1315 – 133218Hemolysin-type calcium-binding 8
Repeat1335 – 135218Hemolysin-type calcium-binding 9
Repeat1411 – 142818Hemolysin-type calcium-binding 10
Repeat1429 – 144618Hemolysin-type calcium-binding 11
Repeat1447 – 146418Hemolysin-type calcium-binding 12
Repeat1468 – 148417Hemolysin-type calcium-binding 13
Repeat1537 – 155418Hemolysin-type calcium-binding 14
Repeat1555 – 157218Hemolysin-type calcium-binding 15
Repeat1573 – 159018Hemolysin-type calcium-binding 16
Repeat1603 – 162018Hemolysin-type calcium-binding 17
Nucleotide binding349 – 3568ATP Potential
Region1 – 399399A, catalytic
Region400 – 912513B, Ala/Gly-rich
Region913 – 1656744C
Region1657 – 170650D, Asp/Gly-rich

Amino acid modifications

Lipidation8601N6-palmitoyl lysine By similarity
Lipidation9831N6-palmitoyl lysine By similarity

Experimental info

Sequence conflict2921A → R in CAA85481. Ref.1
Sequence conflict3711G → R in CAA85481. Ref.1
Sequence conflict546 – 5472AA → G in CAA85481. Ref.1

Hide | Top

Sequences

Sequence LengthMass (Da)Tools
Q57506-1 [UniParc].

Last modified September 19, 2003. Version 4.
Checksum: AF51E8270EA8A68F

FASTA1,706177,056
        10         20         30         40         50         60 
MQQSHQAGYA NAADRESGIP AAVLDGIKAV AKEKNATLMF RLVNPHSTSL IAEGVATKGL 

        70         80         90        100        110        120 
GVHAKSSDWG LQAGYIPVNP NLSKLFGRAP EVIARADNDV NSSLAHGHTA VDLTLSKERL 

       130        140        150        160        170        180 
DYLRQAGLVT GMADGVVASN HAGYEQFEFR VKETSDGRYA VQYRRKGGDD FEAVKVIGNA 

       190        200        210        220        230        240 
AGIPLTADID MFAIMPHLSN FRDSARSSVT SGDSVTDYLA RTRRAASEAT GGLDRERIDL 

       250        260        270        280        290        300 
LWKIARAGAR SAVGTEARRQ FRYDGDMNIG VITDFELEVR NALNRRAHAV GAQDVVQHGT 

       310        320        330        340        350        360 
EQNNPFPEAD EKIFVVSATG ESQMLTRGQL KEYIGQQRGE GYVFYENRAY GVAGKSLFDD 

       370        380        390        400        410        420 
GLGAAPGVPG GRSKSSPDVL ETVPASPGLR RPSLGAVERQ DSGYDSLDGV GSRSFSLGEV 

       430        440        450        460        470        480 
SDMAAVEAAE LEMTRQVLHA GARQDDAEPG VSGASAHWGQ RALQGAQAVA AAQRLVHAIA 

       490        500        510        520        530        540 
LMTQFGRAGS TNTPQEAASL SAAVFGLGEA SSAVAETVSG FFRGSSRWAG GFGVAGGAMA 

       550        560        570        580        590        600 
LGGGIAAAVG AGMSLTDDAP AGQKAAAGAE IALQLTGGTV ELASSIALAL AAARGVTSGL 

       610        620        630        640        650        660 
QVAGASAGAA AGALAAALSP MEIYGLVQQS HYADQLDKLA QESSAYGYEG DALLAQLYRD 

       670        680        690        700        710        720 
KTAAEGAVAG VSAVLSTVGA AVSIAAAASV VGAPVAVVTS LLTGALNGIL RGVQQPIIEK 

       730        740        750        760        770        780 
LANDYARKID ELGGPQAYFE KNLQARHEQL ANSDGLRKML ADLQAGWNAS SVIGVQTTEI 

       790        800        810        820        830        840 
SKSALELAAI TGNADNLKSA DVFVDRFIQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT 

       850        860        870        880        890        900 
FITPLAAPGE EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN 

       910        920        930        940        950        960 
GVLKHSIKLE VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT VSADGERFNV 

       970        980        990       1000       1010       1020 
RKQLNNANVY REGVATQKTA YGKRTENVQY RHVELARVGQ LVEVDTLEHV QHIIGGAGND 

      1030       1040       1050       1060       1070       1080 
SITGNAHDNF LAGGAGDDRL DGGAGNDTLV GGEGHNTVVG GAGDDVFLQD LGVWSNQLDG 

      1090       1100       1110       1120       1130       1140 
GAGVDTVKYN VHQPSEERLE RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSS 

      1150       1160       1170       1180       1190       1200 
LNDSIAGDDR DNELWGDDGN DTIHGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD 

      1210       1220       1230       1240       1250       1260 
IDGGAGLDTV DYSAMIHAGK IVAPHEYGFG IEADLSEGWV RKAARRGMDY YDSVRSVENV 

      1270       1280       1290       1300       1310       1320 
IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD GNDMLYGDAG NDTLYGGLGD 

      1330       1340       1350       1360       1370       1380 
DTLEGGAGND WFGQTPAREH DVLRGGAGVD TVDYSQAGAH AGVATGRIGL GILADLGAGR 

      1390       1400       1410       1420       1430       1440 
VDKLGEAGSS AYDTVSGIEN VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG 

      1450       1460       1470       1480       1490       1500 
DGDDQLSGDA GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG NDTVDFSGPG RGLDAGAKGV 

      1510       1520       1530       1540       1550       1560 
FLSLGKGFAS LMDEPETSNV LRHIENAVGS VRDDVLIGDA GANVLNGLAG NDVLSGGAGD 

      1570       1580       1590       1600       1610       1620 
DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGAGYGHDT IYESGGGHDT IRINAGADQL 

      1630       1640       1650       1660       1670       1680 
WFARQGNDLE IRILGTDDAL TVHDWYRDAD HRVEAIHAAN QAIDPAGIEK LVEAMAQYPD 

      1690       1700 
PGAAAAAPPA ARVPDTLMQS LAVNWR

« Hide

Hide | Top

References

« Hide 'large scale' references
[1]"Cloning and sequence of the Bordetella bronchiseptica adenylate cyclase-hemolysin-encoding gene: comparison with the Bordetella pertussis gene."
Betsou F., Sismeiro O., Danchin A., Guiso N.
Gene 162:165-166(1995) [PubMed: 7557410] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: CIP 9.73.
[2]Danchin A., Boursaux-Eude C.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 1556-1559.
[3]"Comparative analysis of the genome sequences of Bordetella pertussis, Bordetella parapertussis and Bordetella bronchiseptica."
Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R., Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L., Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A., Achtman M., Atkin R., Baker S. expand/collapse author list , Basham D., Bason N., Cherevach I., Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S., Barrell B.G., Maskell D.J.
Nat. Genet. 35:32-40(2003) [PubMed: 12910271] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RB50 / ATCC BAA-588 / NCTC 13252.

Hide | Top

Cross-references

Sequence databases

Z37112 Genomic DNA. Translation: CAA85481.2.
BX640437 Genomic DNA. Translation: CAE30822.1. Different initiation.
PIRS51672.

3D structure databases

HSSPHSSP built from PDB template 1K90 based on UniProtKB P40136.
SMRQ57506. Positions 7-364.
ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus BB0324 in contig BX470250_GR.
KEGGbbr:BB0324.
NMPDRfig|257310.1.peg.320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ57506.

Enzyme and pathway databases

BioCycBBRO257310:BB0324-MON.
BRENDA4.6.1.1. 413.

Family and domain databases

InterProIPR005165. Anthrax_toxin_edema_cen.
IPR001343. Hemolysn_Ca-bd.
IPR018512. Hemolysn_Ca-bd_NodA.
IPR018511. Hemolysn_Ca-bd_sg.
IPR003995. RTX_cytolytic_toxin_protA_bac.
IPR018504. RTX_N.
[Graphical view]
PfamPF03497. Anthrax_toxA. 1 hit.
PF00353. HemolysinCabind. 17 hits.
PF02382. RTX. 1 hit.
[Graphical view]
PRINTSPR00313. CABNDNGRPT.
PR01488. RTXTOXINA.
PROSITEPS00330. HEMOLYSIN_CALCIUM. 5 hits.
[Graphical view]
ProtoNetSearch...

Hide | Top

Entry information

Entry nameCYAA_BORBR
AccessionPrimary (citable) accession number: Q57506
Secondary accession number(s): O05179
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: September 19, 2003
Last modified: June 16, 2009
This is version 70 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Hide | Top

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents