ID A5JW88_BORPT Unreviewed; 1225 AA.
AC A5JW88;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 24-JAN-2024, entry version 54.
DE SubName: Full=Bifunctional hemolysin-adenylate cyclase {ECO:0000313|EMBL:ABQ52218.1};
DE Flags: Fragment;
GN Name=cyaA {ECO:0000313|EMBL:ABQ52218.1};
OS Bordetella pertussis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=520 {ECO:0000313|EMBL:ABQ52218.1};
RN [1] {ECO:0000313|EMBL:ABQ52218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DMST15659 {ECO:0000313|EMBL:ABQ52218.1};
RX PubMed=17846749; DOI=10.1007/s00203-007-0302-1;
RA Powthongchin B., Angsuthanasombat C.;
RT "High level of soluble expression in Escherichia coli and characterisation
RT of the CyaA pore-forming fragment from a Bordetella pertussis Thai clinical
RT isolate.";
RL Arch. Microbiol. 189:169-174(2008).
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
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DR EMBL; EF595960; ABQ52218.1; -; Genomic_DNA.
DR AlphaFoldDB; A5JW88; -.
DR EMDB; EMD-26738; -.
DR SMR; A5JW88; -.
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 107..414
FT /note="RTX pore-forming"
FT /evidence="ECO:0000259|Pfam:PF02382"
FT DOMAIN 1147..1175
FT /note="Haemolysin-type calcium binding-related"
FT /evidence="ECO:0000259|Pfam:PF06594"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABQ52218.1"
SQ SEQUENCE 1225 AA; 126188 MW; 274DE0404F48DB3D CRC64;
MTQFGRAGST NTPQEAASLS AAVFGLGEAS SAVAETVSGF FRGSSRWAGG FGVAGGAMAL
GGGIAAAVGA GMSLTDDAPA GQKAAAGAEI ALQLTGGTVE LASSIALALA AARGVTSGLQ
VAGASAGAAA GALAAALSPM EIYGLVQQSH YADQLDKLAQ ESSAYGYEGD ALLAQLYRDK
TAAEGAVAGV SAVLSTVGAA VSIAAAASVV GAPVAVVTSL LTGALNGILR GVQQPIIEKL
ANDYARKIDE LGGPQAYFEK NLQARHEQLA NSDGLRKMLA DLQAGWNASS VIGVQTTEIS
KSALELAAIT GNADNLKSVD VFVDRFVQGE RVAGQPVVLD VAAGGIDIAS RKGERPALTF
ITPLAAPGEE QRRRTKTGKS EFTTFVEIVG KQDRWRIRDG AADTTIDLAK VVSQLVDANG
VLKHSIKLDV IGGDGDDVVL ANASRIHYDG GAGTNTVSYA ALGRQDSITV SADGERFNVR
KQLNNANVYR EGVATQTTAY GKRTENVQYR HVELARVGQL VEVDTLEHVQ HIIGGAGNDS
ITGNAHDNFL AGGSGDDRLD GGAGNDTLVG GEGQNTVIGG AGDDVFLQDL GVWSNQLDGG
AGVDTVKYNV HQPSEERLER MGDTGIHADL QKGTVEKWPA LNLFSVDHVK NIENLHGSRL
NDRIAGDDQD NELWGHDGND TIRGRGGDDI LRGGLGLDTL YGEDGNDIFL QDDETVSDDI
DGGAGLDTVD YSAMIHPGRI VAPHEYGFGI EADLSREWVR KASALGVDYY DNVRNVENVI
GTSMKDVLIG DAQANTLMGQ GGDDTVRGGD GDDLLFGGDG NDMLYGDAGN DTLYGGLGDD
TLEGGAGNDW FGQTQAREHD VLRGGDGVDT VDYSQTGAHA GIAAGRIGLG ILADLGAGRV
DKLGEAGSSA YDTVSGIENV VGTELADRIT GDAQANVLRG AGGADVLAGG EGDDVLLGGD
GDDQLSGDAG RDRLYGEAGD DWFFQDAANA GNLLDGGDGR DTVDFSGPGR GLDAGAKGVF
LSLGKGFASL MDEPETSNVL RNIENAVGSA RDDVLIGDAG ANVLNGLAGN DVLSGGAGDD
VLLGDEGSDL LSGDAGNDDL FGGQGDDTYL FGVGYGHDTI YESGGGHDTI RINAGADQLW
FARQGNDLEI RILGTDDALT VHDWYRDADH RVEIIHAANQ AVDQAGIEKL VEAMAQYPDP
GAAAAAPPAA RVPDTLMQSL AVNWR
//