CYAD_BORP1
ID CYAD_BORP1 Reviewed; 440 AA.
AC J7QCA7; P11091;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2012, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Protein CyaD;
GN Name=cyaD; OrderedLocusNames=BN118_0470;
OS Bordetella pertussis (strain ATCC 9797 / DSM 5571 / NCTC 10739 / 18323).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=568706;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 9797 / DSM 5571 / NCTC 10739 / 18323;
RX PubMed=2905265; DOI=10.1002/j.1460-2075.1988.tb03288.x;
RA Glaser P., Sakamoto H., Bellalou J., Ullmann A., Danchin A.;
RT "Secretion of cyclolysin, the calmodulin-sensitive adenylate cyclase-
RT haemolysin bifunctional protein of Bordetella pertussis.";
RL EMBO J. 7:3997-4004(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9797 / DSM 5571 / NCTC 10739 / 18323;
RX PubMed=23051057; DOI=10.1186/1471-2164-13-545;
RA Park J., Zhang Y., Buboltz A.M., Zhang X., Schuster S.C., Ahuja U., Liu M.,
RA Miller J.F., Sebaihia M., Bentley S.D., Parkhill J., Harvill E.T.;
RT "Comparative genomics of the classical Bordetella subspecies: the evolution
RT and exchange of virulence-associated diversity amongst closely related
RT pathogens.";
RL BMC Genomics 13:545-545(2012).
CC -!- FUNCTION: CyaD is necessary for transport of calmodulin-sensitive
CC adenylate cyclase-hemolysin (cyclolysin). {ECO:0000269|PubMed:2905265}.
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; X14199; CAA32413.1; -; Genomic_DNA.
DR EMBL; HE965805; CCJ61895.1; -; Genomic_DNA.
DR PIR; S02387; BVBRCD.
DR RefSeq; WP_010929997.1; NC_018518.1.
DR AlphaFoldDB; J7QCA7; -.
DR SMR; J7QCA7; -.
DR STRING; 568706.BN118_0470; -.
DR EnsemblBacteria; CCJ61895; CCJ61895; BN118_0470.
DR GeneID; 45387799; -.
DR KEGG; bper:BN118_0470; -.
DR eggNOG; COG0845; Bacteria.
DR HOGENOM; CLU_023976_0_1_4; -.
DR OMA; EIKPGMP; -.
DR Proteomes; UP000005250; 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 Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..440
FT /note="Protein CyaD"
FT /id="PRO_0000421306"
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"
FT CONFLICT 16
FT /note="L -> V (in Ref. 1; CAA32413)"
FT /evidence="ECO:0000305"
FT CONFLICT 205..206
FT /note="EL -> DV (in Ref. 1; CAA32413)"
FT /evidence="ECO:0000305"
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