ID   RBSA_ECOLI              Reviewed;         501 AA.
AC   P04983; Q2M867;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 180.
DE   RecName: Full=Ribose import ATP-binding protein RbsA {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305};
DE            EC=7.5.2.7 {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:8762140};
GN   Name=rbsA {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000303|PubMed:6327617};
GN   OrderedLocusNames=b3749, JW3728;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=3011793; DOI=10.1016/s0021-9258(19)57448-8;
RA   Bell A.W., Buckel S.D., Groarke J.M., Hope J.N., Kingsley D.H.,
RA   Hermodson M.A.;
RT   "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia
RT   coli K12.";
RL   J. Biol. Chem. 261:7652-7658(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT   organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 1-10, AND DISCUSSION OF SEQUENCE.
RX   PubMed=3086314; DOI=10.1016/s0021-9258(19)57449-x;
RA   Buckel S.D., Bell A.W., Rao J.K.M., Hermodson M.A.;
RT   "An analysis of the structure of the product of the rbsA gene of
RT   Escherichia coli K12.";
RL   J. Biol. Chem. 261:7659-7662(1986).
RN   [6]
RP   PROTEIN SEQUENCE OF 1-6, FUNCTION, ATPASE ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND MUTAGENESIS OF LYS-43.
RX   PubMed=8762140; DOI=10.1002/pro.5560050611;
RA   Barroga C.F., Zhang H., Wajih N., Bouyer J.H., Hermodson M.A.;
RT   "The proteins encoded by the rbs operon of Escherichia coli: I.
RT   Overproduction, purification, characterization, and functional analysis of
RT   RbsA.";
RL   Protein Sci. 5:1093-1099(1996).
RN   [7]
RP   FUNCTION.
RX   PubMed=6327617; DOI=10.1128/jb.158.2.674-682.1984;
RA   Iida A., Harayama S., Iino T., Hazelbauer G.L.;
RT   "Molecular cloning and characterization of genes required for ribose
RT   transport and utilization in Escherichia coli K-12.";
RL   J. Bacteriol. 158:674-682(1984).
RN   [8]
RP   FUNCTION, AND SUBUNIT.
RX   PubMed=25533465; DOI=10.1074/jbc.m114.621573;
RA   Clifton M.C., Simon M.J., Erramilli S.K., Zhang H., Zaitseva J.,
RA   Hermodson M.A., Stauffacher C.V.;
RT   "In vitro reassembly of the ribose ATP-binding cassette transporter reveals
RT   a distinct set of transport complexes.";
RL   J. Biol. Chem. 290:5555-5565(2015).
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, ECO:0000269|PubMed:25533465,
CC       ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:8762140}.
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         ECO:0000305|PubMed:8762140};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=140 uM for ATP {ECO:0000269|PubMed:8762140};
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, ECO:0000269|PubMed:25533465}.
CC   -!- INTERACTION:
CC       P04983; P16685: phnG; NbExp=3; IntAct=EBI-1132449, EBI-9126715;
CC       P04983; P0AGI1: rbsC; NbExp=5; IntAct=EBI-1132449, EBI-21444614;
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01716, ECO:0000305|PubMed:25533465}; Peripheral membrane
CC       protein {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}.
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; M13169; AAA51473.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62102.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC76772.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77539.1; -; Genomic_DNA.
DR   PIR; B26304; B26304.
DR   RefSeq; NP_418205.1; NC_000913.3.
DR   RefSeq; WP_000387770.1; NZ_SSZK01000036.1.
DR   AlphaFoldDB; P04983; -.
DR   SMR; P04983; -.
DR   BioGRID; 4263458; 77.
DR   BioGRID; 852566; 10.
DR   ComplexPortal; CPX-4284; RbsABC ribose ABC transporter.
DR   DIP; DIP-10640N; -.
DR   IntAct; P04983; 13.
DR   STRING; 511145.b3749; -.
DR   TCDB; 3.A.1.2.1; the atp-binding cassette (abc) superfamily.
DR   jPOST; P04983; -.
DR   PaxDb; P04983; -.
DR   PRIDE; P04983; -.
DR   EnsemblBacteria; AAC76772; AAC76772; b3749.
DR   EnsemblBacteria; BAE77539; BAE77539; BAE77539.
DR   GeneID; 948264; -.
DR   KEGG; ecj:JW3728; -.
DR   KEGG; eco:b3749; -.
DR   PATRIC; fig|1411691.4.peg.2951; -.
DR   EchoBASE; EB0807; -.
DR   eggNOG; COG1129; Bacteria.
DR   HOGENOM; CLU_000604_92_3_6; -.
DR   InParanoid; P04983; -.
DR   OMA; AKREIYQ; -.
DR   PhylomeDB; P04983; -.
DR   BioCyc; EcoCyc:RBSA-MON; -.
DR   BioCyc; MetaCyc:RBSA-MON; -.
DR   PRO; PR:P04983; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IDA:EcoCyc.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IPI:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR   GO; GO:0015611; F:ABC-type D-ribose transporter activity; IEA:RHEA.
DR   GO; GO:0015407; F:ABC-type monosaccharide transporter activity; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
DR   GO; GO:0015591; F:D-ribose transmembrane transporter activity; IDA:EcoCyc.
DR   GO; GO:0015752; P:D-ribose transmembrane transport; IDA:ComplexPortal.
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   1: Evidence at protein level;
KW   ATP-binding; Cell inner membrane; Cell membrane; Direct protein sequencing;
KW   Membrane; Nucleotide-binding; Reference proteome; Repeat; Sugar transport;
KW   Translocase; Transport.
FT   CHAIN           1..501
FT                   /note="Ribose import ATP-binding protein RbsA"
FT                   /id="PRO_0000092956"
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"
FT   MUTAGEN         43
FT                   /note="K->R: Loss of transport."
FT                   /evidence="ECO:0000269|PubMed:8762140"
SQ   SEQUENCE   501 AA;  55042 MW;  A37B5F3A910A5D19 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
     KLEDQYPHLD 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