ID C5J4X7_BORBO Unreviewed; 850 AA.
AC C5J4X7;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Adenylate cyclase-hemolysin {ECO:0000313|EMBL:CAQ64441.1};
DE Flags: Fragment;
GN Name=cyaA {ECO:0000313|EMBL:CAQ64441.1};
OS Bordetella bronchiseptica (Alcaligenes bronchisepticus).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=518 {ECO:0000313|EMBL:CAQ64441.1};
RN [1] {ECO:0000313|EMBL:CAQ64441.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FR2011 {ECO:0000313|EMBL:CAQ64441.1};
RA Chenal-Francisque V., Caro V., Boursaux-Eude C., Guiso N.;
RT "Genomic analysis of the adenylate cyclase-hemolysin C-terminal region of
RT Bordetella pertussis, parapertussisand bronchiseptica.";
RL Res. Microbiol. 160:330-336(2009).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; FM165655; CAQ64441.1; -; Genomic_DNA.
DR AlphaFoldDB; C5J4X7; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0015267; F:channel activity; IEA:InterPro.
DR GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; Serralysin-like metalloprotease, C-terminal; 5.
DR InterPro; IPR010566; Haemolys_ca-bd.
DR InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR018504; RTX_pore_form.
DR InterPro; IPR003995; RTX_toxin_determinant-A.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR PANTHER; PTHR38340; S-LAYER PROTEIN; 1.
DR PANTHER; PTHR38340:SF1; S-LAYER PROTEIN; 1.
DR Pfam; PF06594; HCBP_related; 1.
DR Pfam; PF00353; HemolysinCabind; 9.
DR Pfam; PF02382; RTX; 1.
DR PRINTS; PR00313; CABNDNGRPT.
DR PRINTS; PR01488; RTXTOXINA.
DR SUPFAM; SSF51120; beta-Roll; 5.
DR PROSITE; PS00330; HEMOLYSIN_CALCIUM; 5.
PE 4: Predicted;
KW Cytolysis {ECO:0000256|ARBA:ARBA00022852};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Toxin {ECO:0000256|ARBA:ARBA00022656};
KW Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT DOMAIN 1..39
FT /note="RTX pore-forming"
FT /evidence="ECO:0000259|Pfam:PF02382"
FT DOMAIN 772..801
FT /note="Haemolysin-type calcium binding-related"
FT /evidence="ECO:0000259|Pfam:PF06594"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CAQ64441.1"
SQ SEQUENCE 850 AA; 88804 MW; 394702D8B7C13D44 CRC64;
KTGKSEFTTF VEIVGKQDRW RIRDGAADTT IDLAKVVSQL VDANGVLKHS IKLDVIGGDG
DDVVLANASR IHYDGGAGTN TVSYAALGRQ DSITVSADGE RFNVRKQLNN ANVYREGVAT
QTTAYGKRTE NVQYRHVELA RVGQLVEVDT LEHVQHIIGG AGNDSITGNA HDNFLAGGSG
DDRLDGGAGN DTLVGGEGQN TVIGGAGDDV FLQDLGVWSN QLDGGAGVDT VKYNVHQPSE
ERLERMGDTG IHADLQKGTV EKWPALNLFS VDHVKNIENL HGSRLNDRIV GDDRDNELWG
HDGNDTIRGR GGDDILRGGL GLDTLYGEDG NDIFLQDDET VSDDIDGGAG LDTVDYSAMI
HPGRIVAPHE YGFGIEADLS REWVRKASAL GVDYYDNVRN VENVIGTSMK DVLIGDAQAN
TLMGQGGDDT VRGGDGDDLL FGGDGNDMLY GDAGNDTLYG GLGDDTLEGG AGNDWFGQTQ
AREHDVLRGG DGVDTVDYSQ TGAHAGIAAG RIGLGILADL GAGRVDKLGE AGSSAYDTVS
GIENVVGTEL ADRITGDAQA NVLRGAGGAD VLAGGEGDDV LLGGDGDDQL SGDAGRDRLY
GEAGDDWFFQ DAANAGNLLD GGDGRDTVDF SGPGRGLDAG AKGVFLSLGK GFASLMDEPE
TSNVLRHIEN AVGSARDDVL IGDAGANVLN GLAGNDVLSG GAGDDVLLGD EGSDLLSGDA
GNDDLFGGQG DDTYLFGVGY GHDTIYESGG GHDTIRINAG ADQLWFARQG NDLEIRILGT
DDALTVHDWY RDADHRVEAI HAANQAVDQA GIEKLVEAMA QYPDPGAAAA APPAARVPDT
LMQSLAVNWR
//
