ID   RBSA3_RHIEC             Reviewed;         511 AA.
AC   Q2K0S7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Ribose import ATP-binding protein RbsA 3 {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA3 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   OrderedLocusNames=RHE_PE00288;
OS   Rhizobium etli (strain CFN 42 / ATCC 51251).
OG   Plasmid p42e.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=347834;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFN 42 / ATCC 51251;
RX   PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA   Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA   Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA   Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT   "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT   seven interacting replicons.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
CC   -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC       import. Responsible for energy coupling to the transport system.
CC       {ECO:0000255|HAMAP-Rule:MF_01716}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribose(out) + H2O = ADP + D-ribose(in) + H(+) +
CC         phosphate; Xref=Rhea:RHEA:29903, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:47013, ChEBI:CHEBI:456216; EC=7.5.2.7;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01716};
CC   -!- SUBUNIT: The complex is composed of an ATP-binding protein (RbsA), two
CC       transmembrane proteins (RbsC) and a solute-binding protein (RbsB).
CC       {ECO:0000255|HAMAP-Rule:MF_01716}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01716}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01716}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. Ribose importer
CC       (TC 3.A.1.2.1) family. {ECO:0000255|HAMAP-Rule:MF_01716}.
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DR   EMBL; CP000137; ABC93723.1; -; Genomic_DNA.
DR   RefSeq; WP_011428142.1; NC_007765.1.
DR   AlphaFoldDB; Q2K0S7; -.
DR   SMR; Q2K0S7; -.
DR   EnsemblBacteria; ABC93723; ABC93723; RHE_PE00288.
DR   GeneID; 61483271; -.
DR   KEGG; ret:RHE_PE00288; -.
DR   HOGENOM; CLU_000604_92_3_5; -.
DR   OMA; QFMSELV; -.
DR   Proteomes; UP000001936; Plasmid p42e.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR   InterPro; IPR017871; ABC_transporter-like_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00005; ABC_tran; 2.
DR   SMART; SM00382; AAA; 2.
DR   SUPFAM; SSF52540; SSF52540; 2.
DR   PROSITE; PS00211; ABC_TRANSPORTER_1; 1.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS51254; RBSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Plasmid; Reference proteome; Repeat; Sugar transport;
KW   Translocase; Transport.
FT   CHAIN           1..511
FT                   /note="Ribose import ATP-binding protein RbsA 3"
FT                   /id="PRO_0000261082"
FT   DOMAIN          21..257
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          256..511
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         53..60
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   511 AA;  55448 MW;  B732D4031EA34674 CRC64;
     MNAAFQQPVT DSKTGDAPAI LEMRGISQIF PGVKALDNVS IALHPGTVTA LIGENGAGKS
     TLVKILTGIY RPNEGEILVD GQPTSFASAQ AAIDAGVTAI HQETVLFDEL TVAENIFLGH
     APRTRLRTID WQTMNSRSKT LLTALESNID PTIRLKDLSI AQRHLVAIAR ALSIEARIVI
     MDEPTAALSR KEIDDLFRIV RGLKDQGKAI LFISHKFDEL YEIADDFVVF RDGRAVGQGR
     LKETPQDEIV RMMVGRDVEN VFPKIDVAIG GPVLEVEKYC HRTEFRDVSL TLRRGEILGI
     YGLIGAGRSE LAQSLFGVTK PLSGRLTLEG REISINSPHD AIKAGIVYVP EERGRHGLAL
     PMPIYQNMTL PSLARTSRKG FLKAAEEFAL ARKYAERLDL RAAALSVPVG TLSGGNQQKV
     VIGKWLATMP KVIILDEPTK GIDIGSKAAV HGFISELAAE GLSIIMISSE LPEIIGMSDR
     VLVMKEGLSV GLFERDQLSP EALVRAATGN A