ID   RBSA_CALS4              Reviewed;         496 AA.
AC   Q8RD43;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 122.
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=TTE0204;
OS   Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS   11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Caldanaerobacter.
OX   NCBI_TaxID=273068;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4;
RX   PubMed=11997336; DOI=10.1101/gr.219302;
RA   Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA   Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA   Wang J., Yu J., Yang H.;
RT   "A complete sequence of the T. tengcongensis genome.";
RL   Genome Res. 12:689-700(2002).
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 membrane {ECO:0000255|HAMAP-Rule:MF_01716};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-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; AE008691; AAM23505.1; -; Genomic_DNA.
DR   RefSeq; WP_009609666.1; NC_003869.1.
DR   AlphaFoldDB; Q8RD43; -.
DR   SMR; Q8RD43; -.
DR   STRING; 273068.TTE0204; -.
DR   EnsemblBacteria; AAM23505; AAM23505; TTE0204.
DR   KEGG; tte:TTE0204; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_3_9; -.
DR   OMA; AKREIYQ; -.
DR   OrthoDB; 551294at2; -.
DR   Proteomes; UP000000555; 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; 2.
DR   PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
DR   PROSITE; PS51254; RBSA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell membrane; Membrane; Nucleotide-binding;
KW   Reference proteome; Repeat; Sugar transport; Translocase; Transport.
FT   CHAIN           1..496
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000261112"
FT   DOMAIN          5..241
FT                   /note="ABC transporter 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT   DOMAIN          252..496
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   496 AA;  55826 MW;  845B8436FE9BB31E CRC64;
     MEPILQMKGI SKKFGNVKVL DNVDLTLYRG RVLALLGENG AGKSTLMKIL CGIYEKDEGS
     IYLKGKKVNI RNVRDAEKYG IAMIHQELNL VPSLSVAENI FLGREYVRTF NSIDWKKIKQ
     ESAKILHELG MDLNVDRLVK HLSVGEQQMV EIARSLLMNA EILVMDEPTA ALTEGETRRL
     FEVIKRLRKE GKSIIYISHR MNEIFEICDD YIVLRDGCLI SQGEISEVTR DDLVKMMVGR
     ELKEHFPYEC SSPGEEILRV ENLTVKGMFE KVSFVVKKGE VVGFAGLIGA GRTEVAKTIF
     GFYKKTSGKI YLGGEEVKIN SPRDAIEKGI MYLSEDRRNE GLIIKHTLKE NMTLSALKKI
     SDYIGTINFS KERSIVNEMI QKLNIKSFSP NQKIFRLSGG NQQKVAIAKC LLTNPKLIIL
     DEPTRGIDVG AKNEIYKLIN DLKRQGIGII LISSELPEVL NISDRIIVMH EGKITGEISR
     EEATEEKVML KAVGGE