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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_BORBR              Reviewed;        1706 AA.
Q57506; O05179;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
19-SEP-2003, sequence version 4.
05-DEC-2018, entry version 130.
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=BB0324;
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
(Alcaligenes bronchisepticus).
Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
Alcaligenaceae; Bordetella.
NCBI_TaxID=257310;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=CIP 9.73;
PubMed=7557410; DOI=10.1016/0378-1119(95)00339-8;
Betsou F., Sismeiro O., Danchin A., Guiso N.;
"Cloning and sequence of the Bordetella bronchiseptica adenylate
cyclase-hemolysin-encoding gene: comparison with the Bordetella
pertussis gene.";
Gene 162:165-166(1995).
[2]
SEQUENCE REVISION TO 1556-1559.
Danchin A., Boursaux-Eude C.;
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
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).
-!- 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:
Reaction=ATP = 3',5'-cyclic AMP + diphosphate;
Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
ChEBI:CHEBI:58165; EC=4.6.1.1;
-!- 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.
-!- 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}.
-!- SEQUENCE CAUTION:
Sequence=CAE30822.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; Z37112; CAA85481.2; -; Genomic_DNA.
EMBL; BX640437; CAE30822.1; ALT_INIT; Genomic_DNA.
PIR; S51672; S51672.
RefSeq; WP_010925767.1; NC_002927.3.
ProteinModelPortal; Q57506; -.
SMR; Q57506; -.
STRING; 257310.BB0324; -.
PRIDE; Q57506; -.
EnsemblBacteria; CAE30822; CAE30822; BB0324.
KEGG; bbr:BB0324; -.
eggNOG; ENOG4107VZP; Bacteria.
eggNOG; COG2931; LUCA.
HOGENOM; HOG000221187; -.
KO; K22944; -.
OrthoDB; POG091H02L5; -.
Proteomes; UP000001027; Chromosome.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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; IEA:UniProtKB-KW.
Gene3D; 2.150.10.10; -; 7.
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; 8.
Pfam; PF02382; RTX; 1.
PRINTS; PR01488; RTXTOXINA.
SUPFAM; SSF51120; SSF51120; 5.
SUPFAM; SSF81298; SSF81298; 1.
PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
3: Inferred from homology;
ATP-binding; Calcium; Calmodulin-binding; cAMP biosynthesis;
Complete proteome; Cytolysis; Hemolysis; Lipoprotein; Lyase;
Nucleotide-binding; Palmitate; Repeat; Secreted; Toxin; Virulence;
Whooping cough.
CHAIN 1 312 Calmodulin-sensitive adenylate cyclase.
/FTId=PRO_0000001318.
CHAIN 313 1706 Hemolysin. {ECO:0000255}.
/FTId=PRO_0000001319.
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:0000250}.
LIPID 983 983 N6-palmitoyl lysine. {ECO:0000250}.
CONFLICT 292 292 A -> R (in Ref. 1; CAA85481).
{ECO:0000305}.
CONFLICT 371 371 G -> R (in Ref. 1; CAA85481).
{ECO:0000305}.
CONFLICT 546 547 AA -> G (in Ref. 1; CAA85481).
{ECO:0000305}.
SEQUENCE 1706 AA; 177056 MW; AF51E8270EA8A68F 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
GLGAAPGVPG GRSKSSPDVL 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 TGNADNLKSA DVFVDRFIQG ERVAGQPVVL DVAAGGIDIA SRKGERPALT
FITPLAAPGE EQRRRTKTGK SEFTTFVEIV GKQDRWRIRD GAADTTIDLA KVVSQLVDAN
GVLKHSIKLE VIGGDGDDVV LANASRIHYD GGAGTNTVSY AALGRQDSIT VSADGERFNV
RKQLNNANVY REGVATQKTA YGKRTENVQY RHVELARVGQ LVEVDTLEHV QHIIGGAGND
SITGNAHDNF LAGGAGDDRL DGGAGNDTLV GGEGHNTVVG GAGDDVFLQD LGVWSNQLDG
GAGVDTVKYN VHQPSEERLE RMGDTGIHAD LQKGTVEKWP ALNLFSVDHV KNIENLHGSS
LNDSIAGDDR DNELWGDDGN DTIHGRGGDD ILRGGLGLDT LYGEDGNDIF LQDDETVSDD
IDGGAGLDTV DYSAMIHAGK IVAPHEYGFG IEADLSEGWV RKAARRGMDY YDSVRSVENV
IGTSMKDVLI GDAQANTLMG QGGDDTVRGG DGDDLLFGGD GNDMLYGDAG NDTLYGGLGD
DTLEGGAGND WFGQTPAREH DVLRGGAGVD TVDYSQAGAH AGVATGRIGL GILADLGAGR
VDKLGEAGSS AYDTVSGIEN VVGTELADRI TGDAQANVLR GAGGADVLAG GEGDDVLLGG
DGDDQLSGDA GRDRLYGEAG DDWFFQDAAN AGNLLDGGDG NDTVDFSGPG RGLDAGAKGV
FLSLGKGFAS LMDEPETSNV LRHIENAVGS VRDDVLIGDA GANVLNGLAG NDVLSGGAGD
DVLLGDEGSD LLSGDAGNDD LFGGQGDDTY LFGAGYGHDT IYESGGGHDT IRINAGADQL
WFARQGNDLE IRILGTDDAL TVHDWYRDAD HRVEAIHAAN QAIDPAGIEK LVEAMAQYPD
PGAAAAAPPA ARVPDTLMQS LAVNWR


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