ID RBSA_YERPS Reviewed; 507 AA.
AC Q664G2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 128.
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=YPTB3807;
OS Yersinia pseudotuberculosis serotype I (strain IP32953).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=273123;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP32953;
RX PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA Derbise A., Hauser L.J., Garcia E.;
RT "Insights into the evolution of Yersinia pestis through whole-genome
RT comparison with Yersinia pseudotuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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; BX936398; CAH23045.1; -; Genomic_DNA.
DR RefSeq; WP_011193264.1; NZ_CP009712.1.
DR AlphaFoldDB; Q664G2; -.
DR SMR; Q664G2; -.
DR GeneID; 66843771; -.
DR KEGG; ypo:BZ17_2778; -.
DR KEGG; yps:YPTB3807; -.
DR PATRIC; fig|273123.14.peg.2912; -.
DR Proteomes; UP000001011; 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 GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd03216; ABC_Carb_Monos_I; 1.
DR CDD; cd03215; ABC_Carb_Monos_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 PANTHER; PTHR43790; CARBOHYDRATE TRANSPORT ATP-BINDING PROTEIN MG119-RELATED; 1.
DR PANTHER; PTHR43790:SF3; D-ALLOSE IMPORT ATP-BINDING PROTEIN ALSA-RELATED; 1.
DR Pfam; PF00005; ABC_tran; 2.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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..507
FT /note="Ribose import ATP-binding protein RbsA"
FT /id="PRO_0000261122"
FT DOMAIN 7..242
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 253..497
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 507 AA; 55832 MW; E40BB77AE4DF2246 CRC64;
MNKVPLLEMR NITKSFGKFQ ALKGVDLTVF SGEIHALMGE NGAGKSTLMK ILAGAYTTTS
GEILIEGRPW SIKGPKDALN AGISLIYQEM QLAPNLTVAE NIFLGSELSR GGLVQRKEMV
MQTQAVIDRL GAQFKASDLV MGLTIAEQQQ VEIARALHRN SRILVMDEPT AALSTRETHR
LFELILRLRD EGMAIIYISH RMAEVYELSD RVSVLRDGQY VGSLMRANLN ANELVRMMVG
RPLSDLFNKE RDIPLGHLRL NVHHLTDGAK VQAVSLQVRS GEIVGLAGLV GAGRSELAQL
IFGVRKATGG TIEIDGVPLV IHSPREAIRH GIGFLTENRK EQGLFLELAA QDNITMATLE
RDACYGLLDR KKARAISDDA INRLNIRVPH AQVRAGGLSG GNQQKLLISR WVAISPRILI
LDEPTRGVDV GAKSEIYRIM SQMAREGVAI LMISSELPEV VGMSDRVYVM HEGRIAGELH
HPDITQENIM TLATGVTEDH KKEVYHD
//
