ID   PAXB_PASAE              Reviewed;         711 AA.
AC   Q9RCG7;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Exotoxin translocation ATP-binding protein PaxB;
DE            EC=7.4.2.5;
GN   Name=paxB;
OS   Pasteurella aerogenes.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae.
OX   NCBI_TaxID=749;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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: Part of the ABC transporter complex PaxBD involved in PaxA
CC       export. Transmembrane domains (TMD) form a pore in the inner membrane
CC       and the ATP-binding domain (NBD) is responsible for energy generation
CC       (Probable). {ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O + proteinSide 1 = ADP + phosphate + proteinSide 2.;
CC         EC=7.4.2.5;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC       membrane protein {ECO:0000305}.
CC   -!- DOMAIN: In PaxB the peptidase C39 domain, the ATP-binding domain (NBD)
CC       and the transmembrane domain (TMD) are fused.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Protein-1
CC       exporter (TC 3.A.1.109) family. {ECO:0000305}.
CC   -!- CAUTION: Tyr-13 is present instead of the conserved Cys which is
CC       expected to be the active site residue of peptidase C39. Thus this
CC       protein is presumed to be without peptidase activity. {ECO:0000305}.
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DR   EMBL; U66588; AAF15371.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RCG7; -.
DR   SMR; Q9RCG7; -.
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:0015440; F:ABC-type peptide transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0015462; F:ABC-type protein transporter activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008233; F:peptidase activity; IEA:InterPro.
DR   GO; GO:0030253; P:protein secretion by the type I secretion system; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
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 inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Translocase; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN           1..711
FT                   /note="Exotoxin translocation ATP-binding protein PaxB"
FT                   /id="PRO_0000092389"
FT   TRANSMEM        157..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        273..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        299..319
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        392..412
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          1..129
FT                   /note="Peptidase C39"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362"
FT   DOMAIN          158..440
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          472..707
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         506..513
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00362,
FT                   ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   711 AA;  80424 MW;  9A19D2156F648E2E CRC64;
     MEPLMSFKQK NDYGLHALVI LAQYHNIAVS PEEIKHKFDP EGKGIDLVAW LLAAKSFELK
     AKKVKKSIDR LPFIHLPALI WRDDGQHFIL TKIDTQTNRY LIFDLEERNP KVLSAVEFQQ
     VFQGNVILLT SRASIMGKLA KFDFTWFIPA IIKYRKIFVE VMIVSIFLQL FALITPLFFQ
     VVMDKVLVHR GFSTLNVITV ALAIVVIFEI VLSGLRTYVF SHSTSRIDVE LGAKLFRHLL
     ALPISYFENR RVGDTVARVR ELDQIRNFLT GQALTSVLDL LFSFIFFAVM WYYSPKLTIV
     ILLSLPCYIA WSIFISPILR RRLDEKFTRN ADNQAFLVES VTAIDTIKAL AVTPQMTNIW
     DKQLASYVSA DFRVTVLATI GQQGVQLIQK TVMIINLWLG AHLVISGDLS IGQLIAFNML
     SGQVIAPVIR LAQLWQDFQQ VGISITRLGD VLNAPTENFQ GKLSLPEING DVTFKNIRFR
     YKPDAPIILN DVNLTIKQGE VIGIVGRSGS GKSTLTKLLQ RFYIPENGQV LIDGHDLALA
     DPNWLRRQIG VVLQDNVLLN RSIRDNIALT DPSMPMEQVI HAAKLAGAHD FISELREGYN
     TMVGEQGAGL SGGQRQRIAI ARALVNNPRI LIFDEATSAL DYESEHIIMR NMQQICHGRT
     VIIIAHRLST VRKADRIIVM EKGHIVERGK HSELLENKDG LYYYLNQLQS I