ID   RBSA_SHIDS              Reviewed;         495 AA.
AC   Q329G7;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 109.
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=SDY_4128;
OS   Shigella dysenteriae serotype 1 (strain Sd197).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300267;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sd197;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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; CP000034; ABB64038.1; -; Genomic_DNA.
DR   RefSeq; WP_001089404.1; NC_007606.1.
DR   RefSeq; YP_405529.1; NC_007606.1.
DR   AlphaFoldDB; Q329G7; -.
DR   SMR; Q329G7; -.
DR   STRING; 300267.SDY_4128; -.
DR   EnsemblBacteria; ABB64038; ABB64038; SDY_4128.
DR   KEGG; sdy:SDY_4128; -.
DR   PATRIC; fig|300267.13.peg.4852; -.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   OMA; RIDHKAT; -.
DR   Proteomes; UP000002716; 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; 2.
DR   PROSITE; PS51254; RBSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell inner membrane; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW   Translocase; Transport.
FT   CHAIN           1..495
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261102"
FT   DOMAIN          7..242
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          250..491
FT                   /note="ABC transporter 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   BINDING         39..46
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ   SEQUENCE   495 AA;  54032 MW;  2FFB7114B93EF276 CRC64;
     MNSTPVLEMR NIAKAFGKFY ALKGVDLTVY PSENHALMGE NGAGKSTLMK VLAGAYTATS
     GEILIDGKPF HIRTQKDALS AGITLIYQEM QLAPNLSVAE NISLGSELSH GGLVQRKEML
     VQAQKVIDRL GAQFNASDKV MTLTIAEQQQ VEIARALHRN SRILVMDEPT AALSSRETHR
     LFELIMRLRD EGMAIIYISH RMAEVYELSD RVSVLRDGQY VGSLTRDNLN AGELVRMMVG
     RPLSDLFNKE RDIPLGKARL NVHHLTDGGK VQPSSLLVRS GKIVGLAGLV GAGRSELAQL
     IFGVRKATGG MIEVDGEPVV IHSPREAIDL GIGFLTENRK EQGLFLEMAA AENITMATLE
     RDARWEAQTI SDDAIKLLNI RVPHAQVRAG GLSGGNQQKM LISRWVAIGP RILLLDEPTR
     GVDVGAKSEI YRIMNEMARK GVAILMISSE LPEIVGMSDR VYVMHEGSIA GELNGKNITQ
     ENIMTLATGV NDAHS