ID   Y214_RICFE              Reviewed;         576 AA.
AC   Q4UMZ3;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 2.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative export ATP-binding/permease protein RF_0214;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=RF_0214;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY61065.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000053; AAY61065.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_039594812.1; NC_007109.1.
DR   AlphaFoldDB; Q4UMZ3; -.
DR   SMR; Q4UMZ3; -.
DR   STRING; 315456.RF_0214; -.
DR   PRIDE; Q4UMZ3; -.
DR   EnsemblBacteria; AAY61065; AAY61065; RF_0214.
DR   KEGG; rfe:RF_0214; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000008548; 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..576
FT                   /note="Putative export ATP-binding/permease protein
FT                   RF_0214"
FT                   /id="PRO_0000278657"
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..572
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   576 AA;  64466 MW;  23A1B35F732EA3CA CRC64;
     MDIKLLYRLI KYLKFYKKDL IIVMISLLSV SASLLLIGSV FRNLVDNGLS QNHILSVDKS
     ILYICLLIII LSIASFFRSY FINNVAEKAV NQIRKDAYSN LITYEIEEFE ELKIGDIISR
     LTNDIDQIST LIVNFLSFFI RNSVMLIGGV TLMFFESFKL ASIVIITIPI LLIPLIKFGK
     HVKALSKKAL ESKSLLASDI DETFNNIRAI YAFNNQTNKI TDFDTKLQNY LTYCKTRLKI
     RALFFAISIA IIFLAITLVV WIGASDIVKG NLSAGQIISF IYYAIIAGFS SGGIFELLSE
     IHLPLAALER IITIIDKTPI THNSYLELNN SDPISIEFKN VDFTYHSRPN LRIINNMSLK
     INADKFIGIV GRSGGGKSTL MQLLLRFYRQ ESGTILINNQ DITLSNPAEI RKLIAYVPQE
     ANIFSGTIKS NIIFGNTQAS DDDINEIIKI TGIEEFAAKL HDGINAKIGE RGVRLSGGQK
     QRIAIARALL RKPQILLLDE AMSALDTMSE QKLLESIKEI MKGKIIISIA HRISSIESAD
     YILVIDKGGV AASGSHNDLS KNSEIYRNIC REQLTV