ID   Y492_RICBR              Reviewed;         575 AA.
AC   Q1RJ91;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Putative export ATP-binding/permease protein RBE_0492;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=RBE_0492;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: Part of an ABC transporter complex. Transmembrane domains
CC       (TMD) form a pore in the inner membrane and the ATP-binding domain
CC       (NBD) is responsible for energy generation (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC   -!- DOMAIN: The ATP-binding domain (NBD) and the transmembrane domain (TMD)
CC       are fused.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. {ECO:0000305}.
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DR   EMBL; CP000087; ABE04573.1; -; Genomic_DNA.
DR   RefSeq; WP_011477164.1; NC_007940.1.
DR   AlphaFoldDB; Q1RJ91; -.
DR   SMR; Q1RJ91; -.
DR   STRING; 336407.RBE_0492; -.
DR   EnsemblBacteria; ABE04573; ABE04573; RBE_0492.
DR   KEGG; rbe:RBE_0492; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OMA; MSVMMAT; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000001951; 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:0140359; F:ABC-type transporter activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; IPR027417; P-loop_NTPase.
DR   Pfam; PF00664; ABC_membrane; 1.
DR   Pfam; PF00005; ABC_tran; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF90123; SSF90123; 1.
DR   PROSITE; PS50929; ABC_TM1F; 1.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 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..575
FT                   /note="Putative export ATP-binding/permease protein
FT                   RBE_0492"
FT                   /id="PRO_0000278655"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        61..81
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        158..178
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        242..262
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        277..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          20..303
FT                   /note="ABC transmembrane type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   DOMAIN          336..571
FT                   /note="ABC transporter"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         371..378
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
SQ   SEQUENCE   575 AA;  64075 MW;  403065B43162B3DC CRC64;
     MNTKLLYRLA RNLRFYKKDL IIVIISLLSV SLALLLIGNV FRNLVDQGLV LDRTAAVDKS
     ILYICLLIII LSIASFFRSY FINNVAEKVS SQIRKEAYSN LINYEITEFE ELKIGDIISR
     LTSDIDQISK LIVNFLSFFI RNSVMLVGSI ILMFFESFKL ASIVIITIPL LLIPIIKFGK
     HVKALSKKTL ESQSLLASDI NESFSNIKTI HAFGGQAAKI TEFNNLLQDY LTYSAARLKI
     RALFFAFSMA FIFLGVTLVI WIGALDIVKG NLSSGQIISF IYYAIIAGFS SGGIFELLSE
     MHLPLAALER IVTIIDKSPI VHNNYSDLKP VNSISLEFKN VNFSYPSRPN LKILNNISFK
     IDSTQFIGIV GRSGSGKSTL MQLLLRFYVQ ESGIILVNNQ DIALLNPNEI RKLIAYVPQE
     ASIFSGTIKS NIMFGNDSSE EEITEIIKIT GIADFTDKIP DGINAKIGEK GVRLSGGQKQ
     RIALARALLR KPQILLLDEA MNALDSQSEQ KLLSSIRDIM KGKIVISIAH RISSIESADN
     ILIIDKGAVE AEGTHAHLLK TSDLYRTIYK EVDLL