RBSA3_RHIME
ID RBSA3_RHIME Reviewed; 504 AA.
AC Q92UI2;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ribose import ATP-binding protein RbsA 3 {ECO:0000255|HAMAP-Rule:MF_01716};
DE EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716};
GN Name=rbsA3 {ECO:0000255|HAMAP-Rule:MF_01716}; OrderedLocusNames=RB1148;
GN ORFNames=SMb20855;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
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; AL591985; CAC49548.1; -; Genomic_DNA.
DR PIR; D95985; D95985.
DR RefSeq; NP_437688.1; NC_003078.1.
DR RefSeq; WP_010975980.1; NC_003078.1.
DR AlphaFoldDB; Q92UI2; -.
DR SMR; Q92UI2; -.
DR STRING; 266834.SM_b20855; -.
DR EnsemblBacteria; CAC49548; CAC49548; SM_b20855.
DR GeneID; 61601098; -.
DR KEGG; sme:SM_b20855; -.
DR PATRIC; fig|266834.11.peg.6076; -.
DR eggNOG; COG1129; Bacteria.
DR HOGENOM; CLU_000604_92_3_5; -.
DR OMA; KTYAQPV; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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; Plasmid; Reference proteome; Repeat; Sugar transport;
KW Translocase; Transport.
FT CHAIN 1..504
FT /note="Ribose import ATP-binding protein RbsA 3"
FT /id="PRO_0000261090"
FT DOMAIN 6..238
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT DOMAIN 251..494
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01716"
SQ SEQUENCE 504 AA; 54003 MW; D22C8915E8A73861 CRC64;
MVTELANLKS ISKSFGGIHA LRSVNFDVRP GEVHALLGEN GAGKSTLMRV LGGEIIPSQG
EVVINGKRTE LRDPRDARAL GIVVIHQELA LAPDLSVAEN IFLGELPTLI SRFSLRRRAK
QLIDRLGFDI DPGRLVGTLS VAHQQVVEIA KALSQDIKII VFDEPTAVLG AQDAMKLHQI
IRGLRDRGVG IVYISHRLDE VFDIADRMTV MKDGETVGTV ATTDVKIDDI IRMMVGRPIA
NMFPERSQRT IGAELLNVKK LNAGRMVRDV SFSVRAGEIV GLGGLIGSGR TEVARAIFGA
DPLDSGTISL KGKALKLKSP RDAVKAGIGL VPEDRKEHGV VIDKPIRVNA TMARMSSVVN
ALGFLKPALE RTDVTALGKS LRLKASSIDA PVSSLSGGNQ QKVVLAKWFH AGGDVIILDE
PTRGVDVGAK AEIYALINKL AEDGKAVLVI SSEHQELFGL CDRVLAMGQG QIRGELTPSN
YSEENLLGLS MMGGARASNQ GSQV
