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Protein

Bifunctional hemolysin/adenylate cyclase

Gene

cya

Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Enzyme regulationi

Activated by host calmodulin.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi349 – 356ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

  • hemolysis in other organism Source: CACAO
  • pathogenesis Source: UniProtKB-KW
  • positive regulation of cytosolic calcium ion concentration Source: CACAO
Complete GO annotation...

Keywords - Molecular functioni

Lyase, Toxin

Keywords - Biological processi

cAMP biosynthesis, Cytolysis, Hemolysis, Virulence

Keywords - Ligandi

ATP-binding, Calcium, Calmodulin-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional hemolysin/adenylate cyclase
Alternative name(s):
AC-HLY
ACT
Cyclolysin
Cleaved into the following 2 chains:
Alternative name(s):
ATP pyrophosphate-lyase
Adenylyl cyclase
Gene namesi
Name:cya
Synonyms:cyaA
Ordered Locus Names:BP0760
OrganismiBordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Taxonomic identifieri257313 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesAlcaligenaceaeBordetella
Proteomesi
  • UP000002676 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi188D → E, N, Y or H: Loss of activity. 1
Mutagenesisi190D → N, Y or H: Loss of activity. 1
Mutagenesisi298H → R, P or L: Loss of activity. 1
Mutagenesisi301E → Q or K: Loss of activity. 1

Keywords - Diseasei

Whooping cough

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000013201 – 312Calmodulin-sensitive adenylate cyclaseAdd BLAST312
ChainiPRO_0000001321313 – 1706HemolysinSequence analysisAdd BLAST1394

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Lipidationi860N6-palmitoyl lysine1 Publication1
Lipidationi983N6-palmitoyl lysine1 Publication1

Post-translational modificationi

Released in a processed form.
Palmitoylated by CyaC. The toxin only becomes active when modified in position Lys-983.2 Publications

Keywords - PTMi

Lipoprotein, Palmitate

Interactioni

Protein-protein interaction databases

STRINGi257313.BP0760.

Structurei

Secondary structure

11706
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi12 – 16Combined sources5
Helixi21 – 33Combined sources13
Beta strandi36 – 41Combined sources6
Helixi45 – 52Combined sources8
Helixi70 – 72Combined sources3
Beta strandi77 – 79Combined sources3
Helixi80 – 82Combined sources3
Turni84 – 87Combined sources4
Helixi90 – 105Combined sources16
Beta strandi109 – 112Combined sources4
Helixi117 – 125Combined sources9
Beta strandi131 – 138Combined sources8
Helixi142 – 145Combined sources4
Beta strandi147 – 153Combined sources7
Beta strandi159 – 165Combined sources7
Beta strandi168 – 173Combined sources6
Beta strandi175 – 178Combined sources4
Beta strandi184 – 186Combined sources3
Beta strandi191 – 197Combined sources7
Helixi198 – 201Combined sources4
Helixi202 – 209Combined sources8
Beta strandi210 – 212Combined sources3
Helixi215 – 222Combined sources8
Helixi235 – 252Combined sources18
Turni253 – 256Combined sources4
Helixi257 – 259Combined sources3
Beta strandi262 – 264Combined sources3
Beta strandi267 – 271Combined sources5
Helixi274 – 289Combined sources16
Helixi301 – 303Combined sources3
Beta strandi313 – 316Combined sources4
Beta strandi322 – 325Combined sources4
Helixi327 – 339Combined sources13
Turni348 – 354Combined sources7
Beta strandi1535 – 1537Combined sources3
Beta strandi1544 – 1546Combined sources3
Beta strandi1553 – 1555Combined sources3
Beta strandi1562 – 1564Combined sources3
Beta strandi1571 – 1573Combined sources3
Beta strandi1580 – 1582Combined sources3
Beta strandi1589 – 1593Combined sources5
Beta strandi1598 – 1601Combined sources4
Beta strandi1610 – 1615Combined sources6
Helixi1617 – 1619Combined sources3
Beta strandi1620 – 1625Combined sources6
Beta strandi1628 – 1633Combined sources6
Beta strandi1639 – 1642Combined sources4
Turni1643 – 1647Combined sources5
Helixi1649 – 1651Combined sources3
Beta strandi1654 – 1658Combined sources5
Beta strandi1661 – 1664Combined sources4
Helixi1665 – 1674Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRTX-ray2.10A1-364[»]
1YRUX-ray2.50A1-364[»]
1ZOTX-ray2.20A7-364[»]
2COLX-ray2.20A7-362[»]
5CXLX-ray1.45A/B1529-1681[»]
DisProtiDP00591.
ProteinModelPortaliP0DKX7.
SMRiP0DKX7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1014 – 1031Hemolysin-type calcium-binding 1Add BLAST18
Repeati1032 – 1049Hemolysin-type calcium-binding 2Add BLAST18
Repeati1050 – 1067Hemolysin-type calcium-binding 3Add BLAST18
Repeati1155 – 1172Hemolysin-type calcium-binding 4Add BLAST18
Repeati1173 – 1190Hemolysin-type calcium-binding 5Add BLAST18
Repeati1279 – 1296Hemolysin-type calcium-binding 6Add BLAST18
Repeati1297 – 1314Hemolysin-type calcium-binding 7Add BLAST18
Repeati1315 – 1332Hemolysin-type calcium-binding 8Add BLAST18
Repeati1335 – 1352Hemolysin-type calcium-binding 9Add BLAST18
Repeati1411 – 1428Hemolysin-type calcium-binding 10Add BLAST18
Repeati1429 – 1446Hemolysin-type calcium-binding 11Add BLAST18
Repeati1447 – 1464Hemolysin-type calcium-binding 12Add BLAST18
Repeati1468 – 1484Hemolysin-type calcium-binding 13Add BLAST17
Repeati1537 – 1554Hemolysin-type calcium-binding 14Add BLAST18
Repeati1555 – 1572Hemolysin-type calcium-binding 15Add BLAST18
Repeati1573 – 1590Hemolysin-type calcium-binding 16Add BLAST18
Repeati1603 – 1620Hemolysin-type calcium-binding 17Add BLAST18

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 399A, catalyticAdd BLAST399
Regioni400 – 912B, Ala/Gly-richAdd BLAST513
Regioni913 – 1656CAdd BLAST744
Regioni1657 – 1706D, Asp/Gly-richAdd BLAST50

Domaini

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

Sequence similaritiesi

In the N-terminal section; belongs to the adenylyl cyclase class-2 family.Curated
In the C-terminal section; belongs to the RTX prokaryotic toxin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG4107VZP. Bacteria.
COG2931. LUCA.
KOiK11005.
K11029.
OMAiHSLWIGY.

Family and domain databases

Gene3Di2.150.10.10. 6 hits.
InterProiIPR005165. Anthrax_toxin_edema_cen.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR018504. RTX_N.
IPR003995. RTX_toxin_determinant-A.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF03497. Anthrax_toxA. 1 hit.
PF00353. HemolysinCabind. 15 hits.
PF02382. RTX. 1 hit.
[Graphical view]
PRINTSiPR01488. RTXTOXINA.
SUPFAMiSSF51120. SSF51120. 9 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0DKX7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQQSHQAGYA NAADRESGIP AAVLDGIKAV AKEKNATLMF RLVNPHSTSL
60 70 80 90 100
IAEGVATKGL GVHAKSSDWG LQAGYIPVNP NLSKLFGRAP EVIARADNDV
110 120 130 140 150
NSSLAHGHTA VDLTLSKERL DYLRQAGLVT GMADGVVASN HAGYEQFEFR
160 170 180 190 200
VKETSDGRYA VQYRRKGGDD FEAVKVIGNA AGIPLTADID MFAIMPHLSN
210 220 230 240 250
FRDSARSSVT SGDSVTDYLA RTRRAASEAT GGLDRERIDL LWKIARAGAR
260 270 280 290 300
SAVGTEARRQ FRYDGDMNIG VITDFELEVR NALNRRAHAV GAQDVVQHGT
310 320 330 340 350
EQNNPFPEAD EKIFVVSATG ESQMLTRGQL KEYIGQQRGE GYVFYENRAY
360 370 380 390 400
GVAGKSLFDD GLGAAPGVPS GRSKFSPDVL ETVPASPGLR RPSLGAVERQ
410 420 430 440 450
DSGYDSLDGV GSRSFSLGEV SDMAAVEAAE LEMTRQVLHA GARQDDAEPG
460 470 480 490 500
VSGASAHWGQ RALQGAQAVA AAQRLVHAIA LMTQFGRAGS TNTPQEAASL
510 520 530 540 550
SAAVFGLGEA SSAVAETVSG FFRGSSRWAG GFGVAGGAMA LGGGIAAAVG
560 570 580 590 600
AGMSLTDDAP AGQKAAAGAE IALQLTGGTV ELASSIALAL AAARGVTSGL
610 620 630 640 650
QVAGASAGAA AGALAAALSP MEIYGLVQQS HYADQLDKLA QESSAYGYEG
660 670 680 690 700
DALLAQLYRD KTAAEGAVAG VSAVLSTVGA AVSIAAAASV VGAPVAVVTS
710 720 730 740 750
LLTGALNGIL RGVQQPIIEK LANDYARKID ELGGPQAYFE KNLQARHEQL
760 770 780 790 800
ANSDGLRKML ADLQAGWNAS SVIGVQTTEI SKSALELAAI TGNADNLKSV
810 820 830 840 850
DVFVDRFVQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT FITPLAAPGE
860 870 880 890 900
EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN
910 920 930 940 950
GVLKHSIKLD VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT
960 970 980 990 1000
VSADGERFNV RKQLNNANVY REGVATQTTA YGKRTENVQY RHVELARVGQ
1010 1020 1030 1040 1050
LVEVDTLEHV QHIIGGAGND SITGNAHDNF LAGGSGDDRL DGGAGNDTLV
1060 1070 1080 1090 1100
GGEGQNTVIG GAGDDVFLQD LGVWSNQLDG GAGVDTVKYN VHQPSEERLE
1110 1120 1130 1140 1150
RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSR LNDRIAGDDQ
1160 1170 1180 1190 1200
DNELWGHDGN DTIRGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD
1210 1220 1230 1240 1250
IDGGAGLDTV DYSAMIHPGR IVAPHEYGFG IEADLSREWV RKASALGVDY
1260 1270 1280 1290 1300
YDNVRNVENV IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD
1310 1320 1330 1340 1350
GNDMLYGDAG NDTLYGGLGD DTLEGGAGND WFGQTQAREH DVLRGGDGVD
1360 1370 1380 1390 1400
TVDYSQTGAH AGIAAGRIGL GILADLGAGR VDKLGEAGSS AYDTVSGIEN
1410 1420 1430 1440 1450
VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG DGDDQLSGDA
1460 1470 1480 1490 1500
GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG RDTVDFSGPG RGLDAGAKGV
1510 1520 1530 1540 1550
FLSLGKGFAS LMDEPETSNV LRNIENAVGS ARDDVLIGDA GANVLNGLAG
1560 1570 1580 1590 1600
NDVLSGGAGD DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGVGYGHDT
1610 1620 1630 1640 1650
IYESGGGHDT IRINAGADQL WFARQGNDLE IRILGTDDAL TVHDWYRDAD
1660 1670 1680 1690 1700
HRVEIIHAAN QAVDQAGIEK LVEAMAQYPD PGAAAAAPPA ARVPDTLMQS

LAVNWR
Length:1,706
Mass (Da):177,521
Last modified:March 6, 2013 - v1
Checksum:iC1FD3D46CABCEF39
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640413 Genomic DNA. Translation: CAE41066.1.
PIRiS00893. OYBRC.
RefSeqiNP_879578.1. NC_002929.2.
WP_010929995.1. NC_002929.2.

Genome annotation databases

EnsemblBacteriaiCAE41066; CAE41066; BP0760.
GeneIDi2664492.
KEGGibpe:BP0760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX640413 Genomic DNA. Translation: CAE41066.1.
PIRiS00893. OYBRC.
RefSeqiNP_879578.1. NC_002929.2.
WP_010929995.1. NC_002929.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1YRTX-ray2.10A1-364[»]
1YRUX-ray2.50A1-364[»]
1ZOTX-ray2.20A7-364[»]
2COLX-ray2.20A7-362[»]
5CXLX-ray1.45A/B1529-1681[»]
DisProtiDP00591.
ProteinModelPortaliP0DKX7.
SMRiP0DKX7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi257313.BP0760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAE41066; CAE41066; BP0760.
GeneIDi2664492.
KEGGibpe:BP0760.

Phylogenomic databases

eggNOGiENOG4107VZP. Bacteria.
COG2931. LUCA.
KOiK11005.
K11029.
OMAiHSLWIGY.

Family and domain databases

Gene3Di2.150.10.10. 6 hits.
InterProiIPR005165. Anthrax_toxin_edema_cen.
IPR018511. Hemolysin-typ_Ca-bd_CS.
IPR001343. Hemolysn_Ca-bd.
IPR018504. RTX_N.
IPR003995. RTX_toxin_determinant-A.
IPR011049. Serralysin-like_metalloprot_C.
[Graphical view]
PfamiPF03497. Anthrax_toxA. 1 hit.
PF00353. HemolysinCabind. 15 hits.
PF02382. RTX. 1 hit.
[Graphical view]
PRINTSiPR01488. RTXTOXINA.
SUPFAMiSSF51120. SSF51120. 9 hits.
PROSITEiPS00330. HEMOLYSIN_CALCIUM. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCYAA_BORPE
AccessioniPrimary (citable) accession number: P0DKX7
Secondary accession number(s): P15318
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: March 6, 2013
Last modified: November 2, 2016
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.