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Bifunctional hemolysin/adenylate cyclase (AC-HLY) (ACT) (Cyclolysin) [Cleaved into: Calmodulin-sensitive adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase); Hemolysin]

 CYAA_BORPE              Reviewed;        1706 AA.
P0DKX7; P15318;
06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
06-MAR-2013, sequence version 1.
12-SEP-2018, entry version 39.
RecName: Full=Bifunctional hemolysin/adenylate cyclase;
AltName: Full=AC-HLY;
AltName: Full=ACT;
AltName: Full=Cyclolysin;
Contains:
RecName: Full=Calmodulin-sensitive adenylate cyclase;
EC=4.6.1.1;
AltName: Full=ATP pyrophosphate-lyase;
AltName: Full=Adenylyl cyclase;
Contains:
RecName: Full=Hemolysin;
Flags: Precursor;
Name=cya; Synonyms=cyaA; OrderedLocusNames=BP0760;
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257313;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
PubMed=12910271; DOI=10.1038/ng1227;
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., 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.;
"Comparative analysis of the genome sequences of Bordetella pertussis,
Bordetella parapertussis and Bordetella bronchiseptica.";
Nat. Genet. 35:32-40(2003).
[2]
DOMAINS.
PubMed=2007407; DOI=10.1111/j.1432-1033.1991.tb15838.x;
Munier H., Gilles A.-M., Glaser P., Danchin A., Sarfati R., Barzu O.;
"Isolation and characterization of catalytic and calmodulin-binding
domains of Bordetella pertussis adenylate cyclase.";
Eur. J. Biochem. 196:469-474(1991).
[3]
MUTAGENESIS.
PubMed=2542030;
Glaser P., Elmaoglou-Lazaridou A., Krin E., Ladant D., Barzu O.,
Danchin A.;
"Identification of residues essential for catalysis and binding of
calmodulin in Bordetella pertussis adenylate cyclase by site-directed
mutagenesis.";
EMBO J. 8:967-972(1989).
[4]
MUTAGENESIS.
PubMed=2050107;
Glaser P., Munier H., Gilles A.-M., Krin E., Porumb T., Barzu O.,
Sarfati R., Pellecuer C., Danchin A.;
"Functional consequences of single amino acid substitutions in
calmodulin-activated adenylate cyclase of Bordetella pertussis.";
EMBO J. 10:1683-1688(1991).
[5]
REVIEW.
PubMed=8418825;
Danchin A.;
"Phylogeny of adenylyl cyclases.";
Adv. Second Messenger Phosphoprotein Res. 27:109-162(1993).
[6]
PALMITOYLATION AT LYS-983.
PubMed=7939682; DOI=10.1126/science.7939682;
Hackett M., Guo L., Shabanowitz J., Hunt D.F., Hewlett E.L.;
"Internal lysine palmitoylation in adenylate cyclase toxin from
Bordetella pertussis.";
Science 266:433-435(1994).
[7]
PALMITOYLATION AT LYS-860.
PubMed=10196151; DOI=10.1074/jbc.274.16.10777;
Basar T., Havlicek V., Bezouskova S., Halada P., Hackett M., Sebo P.;
"The conserved lysine 860 in the additional fatty-acylation site of
Bordetella pertussis adenylate cyclase is crucial for toxin function
independently of its acylation status.";
J. Biol. Chem. 274:10777-10783(1999).
-!- 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.
-!- ACTIVITY 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. {ECO:0000250}.
-!- PTM: Released in a processed form.
-!- PTM: Palmitoylated by CyaC. The toxin only becomes active when
modified in position Lys-983. {ECO:0000269|PubMed:10196151,
ECO:0000269|PubMed:7939682}.
-!- SIMILARITY: In the N-terminal section; belongs to the adenylyl
cyclase class-2 family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the RTX
prokaryotic toxin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; BX640413; CAE41066.1; -; Genomic_DNA.
PIR; S00893; OYBRC.
RefSeq; NP_879578.1; NC_002929.2.
RefSeq; WP_010929995.1; NC_002929.2.
PDB; 1YRT; X-ray; 2.10 A; A=1-364.
PDB; 1YRU; X-ray; 2.50 A; A=1-364.
PDB; 1ZOT; X-ray; 2.20 A; A=7-364.
PDB; 2COL; X-ray; 2.20 A; A=7-362.
PDB; 5CXL; X-ray; 1.45 A; A/B=1529-1681.
PDBsum; 1YRT; -.
PDBsum; 1YRU; -.
PDBsum; 1ZOT; -.
PDBsum; 2COL; -.
PDBsum; 5CXL; -.
ProteinModelPortal; P0DKX7; -.
SMR; P0DKX7; -.
IntAct; P0DKX7; 1.
STRING; 257313.BP0760; -.
EnsemblBacteria; CAE41066; CAE41066; BP0760.
GeneID; 2664492; -.
KEGG; bpe:BP0760; -.
PATRIC; fig|257313.5.peg.813; -.
eggNOG; ENOG4107VZP; Bacteria.
eggNOG; COG2931; LUCA.
KO; K11005; -.
KO; K11029; -.
OMA; HPGKEGQ; -.
BioCyc; BPER257313:BP0760_11-MONOMER; -.
Proteomes; UP000002676; Chromosome.
GO; GO:0005623; C:cell; IEA:GOC.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0004016; F:adenylate cyclase activity; IDA:CACAO.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008294; F:calcium- and calmodulin-responsive adenylate cyclase activity; IEA:InterPro.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
GO; GO:0006171; P:cAMP biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0044179; P:hemolysis in other organism; IDA:CACAO.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IDA:CACAO.
Gene3D; 2.150.10.10; -; 6.
Gene3D; 3.90.1760.10; -; 1.
InterPro; IPR035099; Anthrax_toxin_C-terminal.
InterPro; IPR005165; Anthrax_toxin_edema_cen.
InterPro; IPR037017; Anthrax_toxin_edema_cen_sf.
InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
InterPro; IPR001343; Hemolysn_Ca-bd.
InterPro; IPR018504; RTX_N.
InterPro; IPR003995; RTX_toxin_determinant-A.
InterPro; IPR011049; Serralysin-like_metalloprot_C.
Pfam; PF03497; Anthrax_toxA; 1.
Pfam; PF00353; HemolysinCabind; 15.
Pfam; PF02382; RTX; 1.
PRINTS; PR01488; RTXTOXINA.
SUPFAM; SSF51120; SSF51120; 9.
SUPFAM; SSF81298; SSF81298; 1.
PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
1: Evidence at protein level;
3D-structure; ATP-binding; Calcium; Calmodulin-binding;
cAMP biosynthesis; Complete proteome; Cytolysis; Hemolysis;
Lipoprotein; Lyase; Nucleotide-binding; Palmitate; Reference proteome;
Repeat; Secreted; Toxin; Virulence; Whooping cough.
CHAIN 1 312 Calmodulin-sensitive adenylate cyclase.
/FTId=PRO_0000001320.
CHAIN 313 1706 Hemolysin. {ECO:0000255}.
/FTId=PRO_0000001321.
REPEAT 1014 1031 Hemolysin-type calcium-binding 1.
REPEAT 1032 1049 Hemolysin-type calcium-binding 2.
REPEAT 1050 1067 Hemolysin-type calcium-binding 3.
REPEAT 1155 1172 Hemolysin-type calcium-binding 4.
REPEAT 1173 1190 Hemolysin-type calcium-binding 5.
REPEAT 1279 1296 Hemolysin-type calcium-binding 6.
REPEAT 1297 1314 Hemolysin-type calcium-binding 7.
REPEAT 1315 1332 Hemolysin-type calcium-binding 8.
REPEAT 1335 1352 Hemolysin-type calcium-binding 9.
REPEAT 1411 1428 Hemolysin-type calcium-binding 10.
REPEAT 1429 1446 Hemolysin-type calcium-binding 11.
REPEAT 1447 1464 Hemolysin-type calcium-binding 12.
REPEAT 1468 1484 Hemolysin-type calcium-binding 13.
REPEAT 1537 1554 Hemolysin-type calcium-binding 14.
REPEAT 1555 1572 Hemolysin-type calcium-binding 15.
REPEAT 1573 1590 Hemolysin-type calcium-binding 16.
REPEAT 1603 1620 Hemolysin-type calcium-binding 17.
NP_BIND 349 356 ATP. {ECO:0000255}.
REGION 1 399 A, catalytic.
REGION 400 912 B, Ala/Gly-rich.
REGION 913 1656 C.
REGION 1657 1706 D, Asp/Gly-rich.
LIPID 860 860 N6-palmitoyl lysine.
{ECO:0000269|PubMed:10196151}.
LIPID 983 983 N6-palmitoyl lysine.
{ECO:0000269|PubMed:7939682}.
MUTAGEN 188 188 D->E,N,Y,H: Loss of activity.
MUTAGEN 190 190 D->N,Y,H: Loss of activity.
MUTAGEN 298 298 H->R,P,L: Loss of activity.
MUTAGEN 301 301 E->Q,K: Loss of activity.
HELIX 12 16 {ECO:0000244|PDB:1YRT}.
HELIX 21 33 {ECO:0000244|PDB:1YRT}.
STRAND 36 41 {ECO:0000244|PDB:1YRT}.
HELIX 45 52 {ECO:0000244|PDB:1YRT}.
HELIX 70 72 {ECO:0000244|PDB:1YRT}.
STRAND 77 79 {ECO:0000244|PDB:1YRT}.
HELIX 80 82 {ECO:0000244|PDB:1YRT}.
TURN 84 87 {ECO:0000244|PDB:1YRT}.
HELIX 90 105 {ECO:0000244|PDB:1YRT}.
STRAND 109 112 {ECO:0000244|PDB:1YRT}.
HELIX 117 125 {ECO:0000244|PDB:1YRT}.
STRAND 131 138 {ECO:0000244|PDB:1YRT}.
HELIX 142 145 {ECO:0000244|PDB:1YRT}.
STRAND 147 153 {ECO:0000244|PDB:1YRT}.
STRAND 159 165 {ECO:0000244|PDB:1YRT}.
STRAND 168 173 {ECO:0000244|PDB:1ZOT}.
STRAND 175 178 {ECO:0000244|PDB:1YRT}.
STRAND 184 186 {ECO:0000244|PDB:1YRT}.
STRAND 191 197 {ECO:0000244|PDB:1YRT}.
HELIX 198 201 {ECO:0000244|PDB:1YRT}.
HELIX 202 209 {ECO:0000244|PDB:1YRT}.
STRAND 210 212 {ECO:0000244|PDB:1YRT}.
HELIX 215 222 {ECO:0000244|PDB:1YRT}.
HELIX 235 252 {ECO:0000244|PDB:1YRT}.
TURN 253 256 {ECO:0000244|PDB:1YRT}.
HELIX 257 259 {ECO:0000244|PDB:1YRT}.
STRAND 262 264 {ECO:0000244|PDB:1YRT}.
STRAND 267 271 {ECO:0000244|PDB:1YRT}.
HELIX 274 289 {ECO:0000244|PDB:1YRT}.
HELIX 301 303 {ECO:0000244|PDB:1YRT}.
STRAND 313 316 {ECO:0000244|PDB:1YRT}.
STRAND 322 325 {ECO:0000244|PDB:1YRT}.
HELIX 327 339 {ECO:0000244|PDB:1YRT}.
TURN 348 354 {ECO:0000244|PDB:1YRT}.
STRAND 1535 1537 {ECO:0000244|PDB:5CXL}.
STRAND 1544 1546 {ECO:0000244|PDB:5CXL}.
STRAND 1553 1555 {ECO:0000244|PDB:5CXL}.
STRAND 1562 1564 {ECO:0000244|PDB:5CXL}.
STRAND 1571 1573 {ECO:0000244|PDB:5CXL}.
STRAND 1580 1582 {ECO:0000244|PDB:5CXL}.
STRAND 1589 1593 {ECO:0000244|PDB:5CXL}.
STRAND 1598 1601 {ECO:0000244|PDB:5CXL}.
STRAND 1610 1615 {ECO:0000244|PDB:5CXL}.
HELIX 1617 1619 {ECO:0000244|PDB:5CXL}.
STRAND 1620 1625 {ECO:0000244|PDB:5CXL}.
STRAND 1628 1633 {ECO:0000244|PDB:5CXL}.
STRAND 1639 1642 {ECO:0000244|PDB:5CXL}.
TURN 1643 1647 {ECO:0000244|PDB:5CXL}.
HELIX 1649 1651 {ECO:0000244|PDB:5CXL}.
STRAND 1654 1658 {ECO:0000244|PDB:5CXL}.
STRAND 1661 1664 {ECO:0000244|PDB:5CXL}.
HELIX 1665 1674 {ECO:0000244|PDB:5CXL}.
SEQUENCE 1706 AA; 177521 MW; C1FD3D46CABCEF39 CRC64;
MQQSHQAGYA NAADRESGIP AAVLDGIKAV AKEKNATLMF RLVNPHSTSL IAEGVATKGL
GVHAKSSDWG LQAGYIPVNP NLSKLFGRAP EVIARADNDV NSSLAHGHTA VDLTLSKERL
DYLRQAGLVT GMADGVVASN HAGYEQFEFR VKETSDGRYA VQYRRKGGDD FEAVKVIGNA
AGIPLTADID MFAIMPHLSN FRDSARSSVT SGDSVTDYLA RTRRAASEAT GGLDRERIDL
LWKIARAGAR SAVGTEARRQ FRYDGDMNIG VITDFELEVR NALNRRAHAV GAQDVVQHGT
EQNNPFPEAD EKIFVVSATG ESQMLTRGQL KEYIGQQRGE GYVFYENRAY GVAGKSLFDD
GLGAAPGVPS GRSKFSPDVL ETVPASPGLR RPSLGAVERQ DSGYDSLDGV GSRSFSLGEV
SDMAAVEAAE LEMTRQVLHA GARQDDAEPG VSGASAHWGQ RALQGAQAVA AAQRLVHAIA
LMTQFGRAGS TNTPQEAASL SAAVFGLGEA SSAVAETVSG FFRGSSRWAG GFGVAGGAMA
LGGGIAAAVG AGMSLTDDAP AGQKAAAGAE IALQLTGGTV ELASSIALAL AAARGVTSGL
QVAGASAGAA AGALAAALSP MEIYGLVQQS HYADQLDKLA QESSAYGYEG DALLAQLYRD
KTAAEGAVAG VSAVLSTVGA AVSIAAAASV VGAPVAVVTS LLTGALNGIL RGVQQPIIEK
LANDYARKID ELGGPQAYFE KNLQARHEQL ANSDGLRKML ADLQAGWNAS SVIGVQTTEI
SKSALELAAI TGNADNLKSV DVFVDRFVQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT
FITPLAAPGE EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN
GVLKHSIKLD VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT VSADGERFNV
RKQLNNANVY REGVATQTTA YGKRTENVQY RHVELARVGQ LVEVDTLEHV QHIIGGAGND
SITGNAHDNF LAGGSGDDRL DGGAGNDTLV GGEGQNTVIG GAGDDVFLQD LGVWSNQLDG
GAGVDTVKYN VHQPSEERLE RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSR
LNDRIAGDDQ DNELWGHDGN DTIRGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD
IDGGAGLDTV DYSAMIHPGR IVAPHEYGFG IEADLSREWV RKASALGVDY YDNVRNVENV
IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD GNDMLYGDAG NDTLYGGLGD
DTLEGGAGND WFGQTQAREH DVLRGGDGVD TVDYSQTGAH AGIAAGRIGL GILADLGAGR
VDKLGEAGSS AYDTVSGIEN VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG
DGDDQLSGDA GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG RDTVDFSGPG RGLDAGAKGV
FLSLGKGFAS LMDEPETSNV LRNIENAVGS ARDDVLIGDA GANVLNGLAG NDVLSGGAGD
DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGVGYGHDT IYESGGGHDT IRINAGADQL
WFARQGNDLE IRILGTDDAL TVHDWYRDAD HRVEIIHAAN QAVDQAGIEK LVEAMAQYPD
PGAAAAAPPA ARVPDTLMQS LAVNWR


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