ID   RBSA2_BURTA             Reviewed;         517 AA.
AC   Q2T8T6;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 109.
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}; OrderedLocusNames=BTH_II0211;
OS   Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS   E264).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=271848;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX   PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA   Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA   DeShazer D.;
RT   "Bacterial genome adaptation to niches: divergence of the potential
RT   virulence genes in three Burkholderia species of different survival
RT   strategies.";
RL   BMC Genomics 6:174-174(2005).
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; CP000085; ABC35218.1; -; Genomic_DNA.
DR   RefSeq; WP_009894904.1; NZ_CP008786.1.
DR   AlphaFoldDB; Q2T8T6; -.
DR   SMR; Q2T8T6; -.
DR   PRIDE; Q2T8T6; -.
DR   EnsemblBacteria; ABC35218; ABC35218; BTH_II0211.
DR   KEGG; bte:BTH_II0211; -.
DR   HOGENOM; CLU_000604_92_3_4; -.
DR   OMA; RIDHKAT; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000001930; 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_0000261053"
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;  54811 MW;  316A810FBE86764B CRC64;
     MQRSDPSRPL LEMRGISKTF PAVRALAGVS LTVHPGEIHS LMGENGAGKS TLIKILSGAY
     QADPGGEILI DGAPISIDGP LAARDAGVAV IYQELCLAPN LTVAENIYVG RELRRGNGRW
     GTIDRAAMAR GCQDVLARLG ADFGPNTLVG TLSIAEQQLV EIARAVHTKA RILVMDEPTT
     PLSSRETENL FRLIRQLRAE GLAIIYISHR MAEIYELSDR VSVLRDGAYV GTLDRDSLSA
     ERLVGMMVGR DISGFYKKAH APYDPGNLLL SVRDVADGGR VRGCSLDLHA GEVLGIAGLV
     GAGRTELARL IFGAEPRVRG EVKLGGKAFG GHSPCDAIDA GLVYLTEDRK RQGLFLDMSV
     RDNINISVCG RDARLGALDL ARGAQRARDA IAALSIRVPH ANVSVGALSG GNQQKVLLSR
     LLETKPRVLI LDEPTRGVDI GAKSEIYRII NDLARAGVGV IVISSELPEI IGVADRVLVM
     REGRVAGELG GHTGAPITQE AIIALATGSS TEAAAAH