CYAB_BORPE
ID CYAB_BORPE Reviewed; 712 AA.
AC P0DKX5; P18770;
DT 06-MAR-2013, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2013, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Cyclolysin secretion/processing ATP-binding protein CyaB;
DE EC=3.4.22.-;
DE EC=7.6.2.-;
GN Name=cyaB; OrderedLocusNames=BP0761;
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: Involved in the export of calmodulin-sensitive adenylate
CC cyclase-hemolysin (cyclolysin). {ECO:0000250}.
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; BX640413; CAE41067.1; -; Genomic_DNA.
DR RefSeq; NP_879579.1; NC_002929.2.
DR RefSeq; WP_010929996.1; NZ_CP039022.1.
DR AlphaFoldDB; P0DKX5; -.
DR SMR; P0DKX5; -.
DR STRING; 257313.BP0761; -.
DR KEGG; bpe:BP0761; -.
DR PATRIC; fig|257313.5.peg.814; -.
DR eggNOG; COG2274; Bacteria.
DR HOGENOM; CLU_000604_95_4_4; -.
DR OMA; ERQRMTI; -.
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: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; Reference proteome; Thiol protease;
KW Translocase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..712
FT /note="Cyclolysin secretion/processing ATP-binding protein
FT CyaB"
FT /id="PRO_0000092239"
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"
SQ SEQUENCE 712 AA; 77646 MW; B942DF3B37706C8C CRC64;
MTSPVAQCAS VPDSGLLCLV MLARYHGLAA DPEQLRHEFA EQAFCSETIQ LAARRVGLKV
RRHRPAPARL PRAPLPAIAL DRQGGYFVLA RFEPGADQAV LIQRPGQAPA RLGQAEFEAL
WAGELLLCAC AASPTQALAR FDFSWFIPAL VKHRHLIGEV LLISLVLQFI ALLTPLFFQV
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
