ID   Y1073_RICCN             Reviewed;         576 AA.
AC   Q92GP9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Putative export ATP-binding/permease protein RC1073;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=RC1073;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03611.1; -; Genomic_DNA.
DR   PIR; A97834; A97834.
DR   RefSeq; WP_010977651.1; NC_003103.1.
DR   AlphaFoldDB; Q92GP9; -.
DR   SMR; Q92GP9; -.
DR   EnsemblBacteria; AAL03611; AAL03611; RC1073.
DR   KEGG; rco:RC1073; -.
DR   PATRIC; fig|272944.4.peg.1229; -.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OMA; RVMHDLR; -.
DR   Proteomes; UP000000816; 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 RC1073"
FT                   /id="PRO_0000278656"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT   TRANSMEM        57..77
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;  64641 MW;  A89B36A9051E2870 CRC64;
     MDIKLLYRLA KYLRCYKKDL IIVMISLLSV SASLLLIGSV FRNLVDKGLS KDHISSVDNS
     ILYICLLIII LSIASFFRSY FINNVAEKAV NQIRKEAYSN LINYEIEEFE ELKIGDIISR
     LTNDIDQIST LIVNFLSFFI RNSVMLIGSI TLMFFESFKL ASIVIITIPI LLIPLIKFGK
     HVKVLSKKAL ESKSLLASDI NETFNNIRAI YAFNHQINKI ADFDTKLQNY LIYCKTRLKI
     RALFFAISIA VIFLAITLVV WIGASDIVKG HLSAGQIISF IYYAIIAGVS CGGIFELLSE
     MHLPVTALER IITIIDKTPI AHNNYLELNN SDPISIEFKN VDFTYHSRPN LRIINNMSLK
     INANKFLGIV GRSGAGKSTV IQLLLRFYRQ ENGTILINNQ DITLLNPAEI RKLIAYVPQE
     ASIFSGTIKS NIIFGNNEAS DDEINEIIKI TGIEEFAAKL HDGINAKIGE RGVRLSGGQK
     QRIAIARALL RMPQILLLDE AMSALDTMSE QKLLESIKKI MRGNIIISIA HRISSIESAD
     YILVIDKGGV VAEGSHNDLS KNSEIYRNIC REQLTI