ID   PAXA_PASAE              Reviewed;        1049 AA.
AC   Q9RCG8;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Exotoxin PaxA;
GN   Name=paxA;
OS   Pasteurella aerogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae.
OX   NCBI_TaxID=749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=JF1319;
RX   PubMed=10603361; DOI=10.1128/iai.68.1.6-12.2000;
RA   Kuhnert P., Heyberger-Meyer B., Nicolet J., Frey J.;
RT   "Characterization of PaxA and its operon: a cohemolytic RTX toxin
RT   determinant from pathogenic Pasteurella aerogenes.";
RL   Infect. Immun. 68:6-12(2000).
CC   -!- FUNCTION: PaxA is associated with abortion cases in swine and
CC       septicemia in young piglets. Shows cohemolytic activity with the
CC       sphingomyelinase of S.aureus but is devoid of direct hemolytic
CC       activity. {ECO:0000269|PubMed:10603361}.
CC   -!- SUBCELLULAR LOCATION: Secreted. Host cell membrane {ECO:0000305};
CC       Multi-pass membrane protein {ECO:0000305}.
CC   -!- DOMAIN: The transmembrane domains are believed to be involved in pore
CC       formation in target cells. {ECO:0000250}.
CC   -!- DOMAIN: The Gly-rich region is probably involved in calcium binding,
CC       which is required for target cell-binding and cytolytic activity.
CC       {ECO:0000250}.
CC   -!- DOMAIN: The C-terminal domain contains an export signal that is
CC       recognized by the ABC transporter complex PaxBD. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RTX prokaryotic toxin (TC 1.C.11) family.
CC       {ECO:0000305}.
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DR   EMBL; U66588; AAF15370.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RCG8; -.
DR   SMR; Q9RCG8; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0020002; C:host cell plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.150.10.10; -; 3.
DR   InterPro; IPR018511; Hemolysin-typ_Ca-bd_CS.
DR   InterPro; IPR001343; Hemolysn_Ca-bd.
DR   InterPro; IPR013550; RTX_C.
DR   InterPro; IPR018504; RTX_N.
DR   InterPro; IPR003995; RTX_toxin_determinant-A.
DR   InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR   Pfam; PF00353; HemolysinCabind; 3.
DR   Pfam; PF02382; RTX; 1.
DR   Pfam; PF08339; RTX_C; 1.
DR   PRINTS; PR01488; RTXTOXINA.
DR   SUPFAM; SSF51120; SSF51120; 1.
DR   PROSITE; PS00330; HEMOLYSIN_CALCIUM; 3.
PE   3: Inferred from homology;
KW   Calcium; Cytolysis; Host cell membrane; Host membrane; Lipoprotein;
KW   Membrane; Repeat; Secreted; Toxin; Transmembrane; Transmembrane helix;
KW   Virulence.
FT   CHAIN           1..1049
FT                   /note="Exotoxin PaxA"
FT                   /id="PRO_0000196236"
FT   TRANSMEM        246..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REPEAT          744..761
FT                   /note="Hemolysin-type calcium-binding 1"
FT   REPEAT          762..779
FT                   /note="Hemolysin-type calcium-binding 2"
FT   REPEAT          780..797
FT                   /note="Hemolysin-type calcium-binding 3"
FT   REPEAT          798..815
FT                   /note="Hemolysin-type calcium-binding 4"
FT   REPEAT          826..843
FT                   /note="Hemolysin-type calcium-binding 5"
FT   REPEAT          844..861
FT                   /note="Hemolysin-type calcium-binding 6"
SQ   SEQUENCE   1049 AA;  112309 MW;  9FA5070E48CC3127 CRC64;
     MSTWSSMLAD LRKQAEIAKQ QAKKGIDVTK NGLQYGVSQV KLQALAAGKS IQKYGNKLVL
     VIPKDYDVNT GNGFFDLAKA AEELGIQVKY IDRNDLEIAH KSLGVTDQFL GLTERGLTLF
     APQLDKFLQQ HSKISNVVGS STGDTVNKLA KSQAIISGVQ SVLGSVLAGI NLNEAIISGG
     SELELAKAGV DLASELVGNI AKGTATIEAF SEQIQNFGKL VQNAKGLGGV GQQLQHISGS
     ALSKTGLGLD IISSLLSGVT ASFTLADKNA STSTKVAAGF ELSNQVIGGI TKAVSSYILA
     QRLAAGLSTT GPAAALIASS ISLAISPLSF LRVADNFNRS KDIREFAERF KKLGYEGDKL
     LSDFYHEAGT IDASITTIST ALSAIAAGTA AASAGALVGA PITLLVTGIT GLISGILEFS
     KQPMLEHVAS KLGTKIEEWE RKYGKNYFEN GYDARHKAFL EDSLSLLSSF NKQYETERAV
     LITQQRWDEY IGELAGVTGK GDKISSGKAY VDYFEEGKLL AKKPDDFNRV ILDPKKGKID
     ISNSQTSTLL KFVTPLLTPG TESRKRTQTG KYEYVTKLDV NGINQWEVNG VKEKGAVYDF
     TNLIQHVHIS SSVARGEEYR EVRLVSRLGK GNDKVFLASG SAEIHAGDGH DVVYYDKTDT
     GLLMVDGTQA TKQGDYTVTR ELSGATQILR EVVKNQKSSV GSRQETVEYR DNELAQSGNS
     NLKAKDNLYS VEEIIGSNHR DEFKGSKFRD IFHGADGDDL LNGNDGDDIL YGDKGNDELR
     GDNGNDQLYG GEGNDKLFGG NGNNYLSGGD GDDELQVLGN GFNVLRGGKG NDKLYGGAGS
     DFLDGGEGDD YLAGGEGNDF YVYRSTSGNH TIYDQGKSSD SDTLYLSDLT FDRLLVEKVD
     NNLVFKPSDH NSNRGSLTIK DWFKTGHGYN HKLEQIVDKN GRKLTSDNLE THFNGTPKTN
     LLGYTAENQN ESNLSSLKTE LGKIISSAGN FGLAKQGNNN HSAALNNDVD KLISSASSFA
     TAQMGGSGIG LLPSNNANST ILSGLARTA