ID   RBSA_ECOUT              Reviewed;         501 AA.
AC   Q1R4I3;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN   Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=UTI89_C4304;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(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; CP000243; ABE09731.1; -; Genomic_DNA.
DR   RefSeq; WP_000387779.1; NC_007946.1.
DR   AlphaFoldDB; Q1R4I3; -.
DR   SMR; Q1R4I3; -.
DR   PRIDE; Q1R4I3; -.
DR   EnsemblBacteria; ABE09731; ABE09731; UTI89_C4304.
DR   KEGG; eci:UTI89_C4304; -.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   OMA; AKREIYQ; -.
DR   Proteomes; UP000001952; Chromosome.
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; 1.
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..501
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261063"
FT   DOMAIN          5..241
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          252..495
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         37..44
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   501 AA;  55041 MW;  217B5F38330A5D1D CRC64;
     MEALLQLKGI DKAFPGVKAL SGAALNVYPG RVMALVGENG AGKSTMMKVL TGIYTRDAGT
     LLWLGKETTF TGPKSSQEAG IGIIHQELNL IPQLTIAENI FLGREFVNRF GKIDWKTMYA
     EADKLLAKLN LRFKSDKLVG DLSIGDQQMV EIAKVLSFES KVIIMDEPTD ALTDTETESL
     FRVIRELKSQ GRGIVYISHR MKEIFEICDD VTVFRDGQFI AEREVASLTE DSLIEMMVGR
     KLEDQYPHLN KAPGDIRLKV DNLCGPGVND VSFTLRKGEI LGVSGLMGAG RTELMKVLYG
     ALPRTSGYVT LDGHEVVTRS PQDGLANGIV YISEDRKRDG LVLGMSVKEN MSLTALRYFS
     RAGGSLKHAD EQQAVSDFIR LFNVKTPSME QAIGLLSGGN QQKVAIARGL MTRPKVLILD
     EPTRGVDVGA KKEIYQLINQ FKADGLSIIL VSSEMPEVLG MSDRIIVMHE GHLSGEFTRE
     QATQEVLMAA AVGKLNRVNQ E