ID   RBSA2_BURP1             Reviewed;         517 AA.
AC   Q3JHZ1;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Ribose import ATP-binding protein RbsA 2 {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA2 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   OrderedLocusNames=BURPS1710b_A1655;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000125; ABA51846.1; -; Genomic_DNA.
DR   RefSeq; WP_004537694.1; NC_007435.1.
DR   AlphaFoldDB; Q3JHZ1; -.
DR   SMR; Q3JHZ1; -.
DR   EnsemblBacteria; ABA51846; ABA51846; BURPS1710b_A1655.
DR   GeneID; 56531409; -.
DR   KEGG; bpm:BURPS1710b_A1655; -.
DR   HOGENOM; CLU_000604_92_3_4; -.
DR   OMA; RIDHKAT; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000002700; Chromosome II.
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; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..517
FT                   /note="Ribose import ATP-binding protein RbsA 2"
FT                   /id="PRO_0000261049"
FT   DOMAIN          11..251
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          263..507
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   517 AA;  55266 MW;  295A03479F07CC09 CRC64;
     MQRSDPPRPL LEMRGISKTF PAVRALAGVS LTVHPGEVHS LMGENGAGKS TLMKILSGAY
     QADPGGEILI DGRPISIDGP LAAREAGVAV IYQELCLAPN LSVAENIHVG RELRRGNGRR
     GTIDRAAMAR GCQDVLERLG ADFGPNTLVG TLSIAEQQLV EIARAVHTRA RILVMDEPTT
     PLSSRETDNL FRLIRQLRAE GLAIIYISHR MAEIYELSDR VSVLRDGAYV GTLERDALSA
     ERLVGMMVGR DISGFYKKAH APYDPGNLLL SVRDIADGAR VRGCSLDLHA GEVLGIAGLV
     GAGRTELARL IFGAEPRVRG EVTLAGKAFA AHSPREAIDA GLVYLTEDRK RQGLFLDMSV
     RENINISVCG RDARLGALDL ARGAQRARDA IAALSIRVPH ANVNVGALSG GNQQKVLLSR
     LLETKPRVLI LDEPTRGVDI GAKSEIYRII NELARAGVGV IVISSELPEI IGVADRVLVM
     REGRIAGELG GRTDAPITQE AIIALATGSR TEASAAH