CYAD_BORPE
ID CYAD_BORPE Reviewed; 440 AA.
AC P0DKX9; P11091;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 25-MAY-2022, entry version 38.
DE RecName: Full=Protein CyaD;
GN Name=cyaD; OrderedLocusNames=BP0762;
OS Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257313;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX PubMed=12910271; DOI=10.1038/ng1227;
RA Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA Barrell B.G., Maskell D.J.;
RT "Comparative analysis of the genome sequences of Bordetella pertussis,
RT Bordetella parapertussis and Bordetella bronchiseptica.";
RL Nat. Genet. 35:32-40(2003).
CC -!- FUNCTION: CyaD is necessary for transport of calmodulin-sensitive
CC adenylate cyclase-hemolysin (cyclolysin). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Single-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC family. {ECO:0000305}.
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DR EMBL; BX640413; CAE41068.1; -; Genomic_DNA.
DR RefSeq; NP_879580.1; NC_002929.2.
DR RefSeq; WP_010929997.1; NZ_CP039022.1.
DR AlphaFoldDB; P0DKX9; -.
DR SMR; P0DKX9; -.
DR STRING; 257313.BP0762; -.
DR GeneID; 45387799; -.
DR KEGG; bpe:BP0762; -.
DR PATRIC; fig|257313.5.peg.815; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_023976_0_1_4; -.
DR OMA; EIKPGMP; -.
DR Proteomes; UP000002676; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR InterPro; IPR006144; Secretion_HlyD_CS.
DR InterPro; IPR010129; T1SS_HlyD.
DR Pfam; PF13533; Biotin_lipoyl_2; 1.
DR TIGRFAMs; TIGR01843; type_I_hlyD; 1.
DR PROSITE; PS00543; HLYD_FAMILY; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Cytolysis; Hemolysis; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..440
FT /note="Protein CyaD"
FT /id="PRO_0000201866"
FT TOPO_DOM 1..55
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..440
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
SQ SEQUENCE 440 AA; 48054 MW; 27B773B66BD00FF3 CRC64;
MRRALRELAA RHGRVLAASW RQRHRRPAGW FDPVETEFLP SALSLQERPI SPTARWLARI
LMALAAGALV WSVVGKTEIV VHAAGKVVPV GQSKIIAASE TGRVARVLVA DNSRVAAGDV
LLRLDAGVTE AEERKWRVQA AQARQDEARS RAMIRALDTG RAPVLAELPA DPGMMAAQSY
LDSQYADYQA QLRSIEAAIA TYRRELGLVT QIAHAHRGLR RDGDVSQQAY LEKEQARMTL
EGRLRQSEAQ RAALQTQTRR QAFETLVLAR KLAAQAEQEI ARTSAQRSRL VLTAPVDGVV
QQLVALTEGT AVAATQPLMM VVPSGAGIQV QAQLDSKDIG FVRAGAPATV KVGAYDYTKY
GTLEGKVLYV SPDTVVDDRQ QHSYRVTIAL AHPALEVDGK PRLLKEGMAV QADIRTGSRR
LIEYLLSPVA RHAGESLGER