CYAB_BORP1
ID CYAB_BORP1 Reviewed; 712 AA.
AC P0DKX6; P18770;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Cyclolysin secretion/processing ATP-binding protein CyaB;
DE EC=3.4.22.-;
DE EC=7.6.2.-;
GN Name=cyaB; OrderedLocusNames=BN118_0469;
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: Involved in the export of calmodulin-sensitive adenylate
CC cyclase-hemolysin (cyclolysin). {ECO:0000269|PubMed:2905265}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Cyclolysin
CC exporter (TC 3.A.1.109.2) family. {ECO:0000305}.
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DR EMBL; X14199; CAA32412.1; -; Genomic_DNA.
DR EMBL; HE965805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; S02386; BVBRCB.
DR RefSeq; WP_041166126.1; NC_018518.1.
DR AlphaFoldDB; P0DKX6; -.
DR SMR; P0DKX6; -.
DR GeneID; 45387798; -.
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:0030256; C:type I protein secretion system complex; IEA:InterPro.
DR GO; GO:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
DR GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd02417; Peptidase_C39_likeA; 1.
DR Gene3D; 1.20.1560.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR011527; ABC1_TM_dom.
DR InterPro; IPR036640; ABC1_TM_sf.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR017871; ABC_transporter-like_CS.
DR InterPro; IPR010132; ATPase_T1SS_HlyB.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005074; Peptidase_C39.
DR InterPro; IPR039395; Peptidase_C39-like_A.
DR InterPro; IPR039421; Type_1_exporter.
DR PANTHER; PTHR24221; PTHR24221; 1.
DR Pfam; PF00664; ABC_membrane; 1.
DR Pfam; PF00005; ABC_tran; 1.
DR Pfam; PF03412; Peptidase_C39; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF90123; SSF90123; 1.
DR TIGRFAMs; TIGR01846; type_I_sec_HlyB; 1.
DR PROSITE; PS50929; ABC_TM1F; 1.
DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1.
DR PROSITE; PS50990; PEPTIDASE_C39; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Cytolysis; Hemolysis; Hydrolase; Membrane;
KW Nucleotide-binding; Protease; Thiol protease; Translocase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..712
FT /note="Cyclolysin secretion/processing ATP-binding protein
FT CyaB"
FT /id="PRO_0000421302"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 194..214
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 367..387
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 7..128
FT /note="Peptidase C39"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT DOMAIN 157..439
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 471..706
FT /note="ABC transporter"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 505..512
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT ECO:0000255|PROSITE-ProRule:PRU00434"
FT CONFLICT 90
FT /note="A -> VP (in Ref. 1; CAA32412)"
FT /evidence="ECO:0000305"
FT CONFLICT 198
FT /note="A -> T (in Ref. 1; CAA32412)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="D -> H (in Ref. 1; CAA32412)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..406
FT /note="VALGVLWVGATEVVAQ -> LRWESCGWAHRGGRA (in Ref. 1;
FT CAA32412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 712 AA; 77662 MW; E928BF3B37775820 CRC64;
MTSPVAQCAS VPDSGLLCLV MLARYHGLAA DPEQLRHEFA EQAFCSETIQ LAARRVGLKV
RRHRPAPARL PRAPLPAIAL DRQGGYFVLA RFEPGADQAV LIQRPGQAPA RLGQAEFEAL
WAGELLLCAC AASPTQALAR FDFSWFIPAL VKHRHLIGEV LLISLVLQFI SLLTPLFFQV
VMDKVLVNNA METLNVIAVG FLAAILFEAL LTGIRTYLFA HTSSKLDVEL GARLYAHLLR
LPLAYFQARR VGDSVARVRE LEHIRAFLTG NAVTVLLDVV FSVVFIAVMF FYSVKLTLVV
LAALPCYFLL SLVLTPVLRR RLDVKFNRGA ENQAFLVETV SGIDTVKSLA VEPQWQRNWD
RQLAGYVAAG LSVANVAMLA NTGVTLISRL VALGVLWVGA TEVVAQRMTV GELVAFNMLS
GHVTQPVIRL AQLWNDFQQT GVSMQRLGDI LNCRTEVAGD KAQLPALRGS IELDRVSFRY
RPDAADALRN VSLRIAPGEV VGVVGRSGSG KSTLTRLIQR MFVADRGRVL IDGHDIGIVD
SASLRRQLGV VLQESTLFNR SVRDNIALTR PGASMHEVVA AARLAGAHEF ICQLPEGYDT
MLGENGVGLS GGQRQRIGIA RALIHRPRVL ILDEATSALD YESEHIIQRN MRDICDGRTV
IIIAHRLSAV RCADRIVVME GGEVAECGSH ETLLAAGGLY ARLQALQAGE AG
