ID   Y691_RICTY              Reviewed;         576 AA.
AC   Q68W42;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Putative export ATP-binding/permease protein RT0691;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=RT0691;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04150.1; -; Genomic_DNA.
DR   RefSeq; WP_011191127.1; NC_006142.1.
DR   AlphaFoldDB; Q68W42; -.
DR   SMR; Q68W42; -.
DR   STRING; 257363.RT0691; -.
DR   EnsemblBacteria; AAU04150; AAU04150; RT0691.
DR   KEGG; rty:RT0691; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OMA; MSVMMAT; -.
DR   OrthoDB; 643917at2; -.
DR   Proteomes; UP000000604; 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 RT0691"
FT                   /id="PRO_0000278659"
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;  64924 MW;  AFF833C7258A6696 CRC64;
     MDIKLLYRLA KYLRFYKKDL IIVMISLLSV SASLLLIGSV FRNLIDKGLA EDNILSVNKS
     ILYICLLIVI LSVASFFRSY FINNVAEKIV NQIRKEAYSN LINYEIEEYE ELKIGDIISR
     LTNDIDQIAT LIVNFLSFFI RNSVMLIGGI TLMFFESFKL ASIVIVTIPI LLVPLIKFGK
     HVKSLSKKAL ESKSLLVSDI DETFNNIRVI YAFNHQINKI SDFDTKLQSY LIYCKIRLKI
     RALFFAISIA VIFLTITLIV WIGASDIVQG DLSAGQIISF IYYAIIAGVS SGGIFELLSE
     IHLPTTALER IITIIDKISI VHNNYYALNN PDTVSIEFKN VDFTYNSRPN LKIINNMSLK
     INANKFVGIV GRSGAGKSTL IQLLLRFYRQ DNGTILINNQ DISRINPTDI RKFIAYVPQE
     ASIFSDTIKS NIIFGNNKAS DYEINEIIKI TGIEEFSNKL HDGINTKIGE KGVRLSGGQK
     QRIAIARALL RKPKILLLDE AMSALDTMSE QKLLNAIKKI MKGNIIISIA HRISSIESAD
     YILVIDKGKV VTAGSHYDLS KNSEIYRNIC REQLTI