ID   Y696_RICPR              Reviewed;         576 AA.
AC   Q9ZCM8;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Putative export ATP-binding/permease protein RP696;
DE            EC=7.-.-.-;
GN   OrderedLocusNames=RP696;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
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; AJ235272; CAA15132.1; -; Genomic_DNA.
DR   PIR; B71676; B71676.
DR   RefSeq; NP_221056.1; NC_000963.1.
DR   RefSeq; WP_010886351.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZCM8; -.
DR   SMR; Q9ZCM8; -.
DR   STRING; 272947.RP696; -.
DR   EnsemblBacteria; CAA15132; CAA15132; CAA15132.
DR   GeneID; 57569821; -.
DR   KEGG; rpr:RP696; -.
DR   PATRIC; fig|272947.5.peg.717; -.
DR   eggNOG; COG1132; Bacteria.
DR   HOGENOM; CLU_000604_84_3_5; -.
DR   OMA; MSVMMAT; -.
DR   Proteomes; UP000002480; 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; Reference proteome; Translocase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..576
FT                   /note="Putative export ATP-binding/permease protein RP696"
FT                   /id="PRO_0000278658"
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;  64928 MW;  E99C360532E4073F CRC64;
     MDIKLLYRLA KYLRFYKKDL IIVMISLLSV SASLLLIGSI FRDLIDRGLA EDNILSVNKS
     ILYICLLIVI LSVASFFRSY FINNVAEKIV NQIRKEAYSN LINYEIEEYE ELKIGDIISR
     LTNDIDQIAT LIVNFLSFFI RNSVMLIGSI TLMFFESFKL ASIVIITIPI LLVPLIKFGK
     HVKALSKKAL ESKSLLVSDI DETFNNIRVI YAFNHQINKI ADFDTKLQSY LIYCKTRLKI
     RALFFAISIA VIFLTITLIV WIGASDIVQG DLSAGQIISF IYYAIIAGVS SGGIFELLSE
     MHLPTTALER IITIIDKTSI VHNNYYALNN SDAISIEFKN VDFTYNSRPN LKVINNMSLK
     INSNKFVGIV GRSGAGKSTL IQLLLRFYRQ ENGTILINNQ DISFVKPTDI RKFIAYVPQE
     ASIFSDTIKS NIIFGNNKAS DYEINEIIKI TGIEEFSTKL HDGINTKIGE KGVRLSGGQK
     QRIAIARALL RKPKILLLDE AMSALDTMSE QKLLNAIKKI MKGNIIISIA HRISSIESAD
     YILVIDKGGV VTEGSHYDLS KNSEIYRNIC REQLTI