RBSB_ECOLI
ID RBSB_ECOLI Reviewed; 296 AA.
AC P02925; Q2M869;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=Ribose import binding protein RbsB {ECO:0000305};
DE Flags: Precursor;
GN Name=rbsB {ECO:0000303|PubMed:6327617}; Synonyms=prlB, rbsP;
GN OrderedLocusNames=b3751, JW3730;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=6313683; DOI=10.1016/s0021-9258(17)44063-4;
RA Groarke J.M., Mahoney W.C., Hope J.N., Furlong C.E., Robb F.T., Zalkin H.,
RA Hermodson M.A.;
RT "The amino acid sequence of D-ribose-binding protein from Escherichia coli
RT K12.";
RL J. Biol. Chem. 258:12952-12956(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Mauzy C.A.;
RL Submitted (FEB-1986) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
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 [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-296.
RC STRAIN=K12;
RX PubMed=3011794; DOI=10.1016/s0021-9258(19)57450-6;
RA Hope J.N., Bell A.W., Hermodson M.A., Groarke J.M.;
RT "Ribokinase from Escherichia coli K12. Nucleotide sequence and
RT overexpression of the rbsK gene and purification of ribokinase.";
RL J. Biol. Chem. 261:7663-7668(1986).
RN [8]
RP PROTEIN SEQUENCE OF 26-39.
RC STRAIN=K12;
RX PubMed=8899705; DOI=10.1111/j.1365-2958.1996.tb02652.x;
RA Gonzalez-Gil G., Bringmann P., Kahmann R.;
RT "FIS is a regulator of metabolism in Escherichia coli.";
RL Mol. Microbiol. 22:21-29(1996).
RN [9]
RP PROTEIN SEQUENCE OF 26-37.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [10]
RP FUNCTION.
RX PubMed=4608146; DOI=10.1016/s0021-9258(19)42146-7;
RA Willis R.C., Furlong C.E.;
RT "Purification and properties of a ribose-binding protein from Escherichia
RT coli.";
RL J. Biol. Chem. 249:6926-6929(1974).
RN [11]
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 [12]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [13]
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).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS), AND SUBCELLULAR LOCATION.
RX PubMed=1583688; DOI=10.1016/0022-2836(92)91033-l;
RA Mowbray S.L., Cole L.B.;
RT "1.7-A X-ray structure of the periplasmic ribose receptor from Escherichia
RT coli.";
RL J. Mol. Biol. 225:155-175(1992).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), AND FUNCTION.
RX PubMed=7982928; DOI=10.1016/s0021-9258(18)43798-2;
RA Bjoerkman A.J., Binnie R.A., Zhang H., Cole L.B., Hermodson M.A.,
RA Mowbray S.L.;
RT "Probing protein-protein interactions. The ribose-binding protein in
RT bacterial transport and chemotaxis.";
RL J. Biol. Chem. 269:30206-30211(1994).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=9641984; DOI=10.1006/jmbi.1998.1785;
RA Bjoerkman A.J., Mowbray S.L.;
RT "Multiple open forms of ribose-binding protein trace the path of its
RT conformational change.";
RL J. Mol. Biol. 279:651-664(1998).
CC -!- FUNCTION: Part of the ABC transporter complex RbsABC involved in ribose
CC import. Binds ribose. Also serves as the primary chemoreceptor for
CC chemotaxis. {ECO:0000269|PubMed:25533465, ECO:0000269|PubMed:4608146,
CC ECO:0000269|PubMed:6327617, ECO:0000269|PubMed:7982928}.
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:0000269|PubMed:25533465}.
CC -!- INTERACTION:
CC P02925; P00956: ileS; NbExp=3; IntAct=EBI-369930, EBI-552928;
CC P02925; P0AGI1: rbsC; NbExp=6; IntAct=EBI-369930, EBI-21444614;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1583688}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC {ECO:0000305}.
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DR EMBL; K00511; AAA50966.1; -; Genomic_DNA.
DR EMBL; M13169; AAA51475.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62104.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76774.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77537.1; -; Genomic_DNA.
DR PIR; A03425; JGECR.
DR RefSeq; NP_418207.1; NC_000913.3.
DR RefSeq; WP_001056271.1; NZ_LN832404.1.
DR PDB; 1BA2; X-ray; 2.10 A; A/B=26-296.
DR PDB; 1DBP; X-ray; 2.20 A; A=26-296.
DR PDB; 1DRJ; X-ray; 2.50 A; A=26-296.
DR PDB; 1DRK; X-ray; 2.00 A; A=26-296.
DR PDB; 1URP; X-ray; 2.30 A; A/B/C/D=26-296.
DR PDB; 2DRI; X-ray; 1.60 A; A=26-296.
DR PDB; 2GX6; X-ray; 1.97 A; A=26-296.
DR PDBsum; 1BA2; -.
DR PDBsum; 1DBP; -.
DR PDBsum; 1DRJ; -.
DR PDBsum; 1DRK; -.
DR PDBsum; 1URP; -.
DR PDBsum; 2DRI; -.
DR PDBsum; 2GX6; -.
DR AlphaFoldDB; P02925; -.
DR SMR; P02925; -.
DR BioGRID; 4262120; 64.
DR BioGRID; 852563; 9.
DR ComplexPortal; CPX-4284; RbsABC ribose ABC transporter.
DR DIP; DIP-10641N; -.
DR IntAct; P02925; 18.
DR MINT; P02925; -.
DR STRING; 511145.b3751; -.
DR DrugBank; DB04286; beta-D-Ribopyranose.
DR TCDB; 3.A.1.2.1; the atp-binding cassette (abc) superfamily.
DR SWISS-2DPAGE; P02925; -.
DR jPOST; P02925; -.
DR PaxDb; P02925; -.
DR PRIDE; P02925; -.
DR EnsemblBacteria; AAC76774; AAC76774; b3751.
DR EnsemblBacteria; BAE77537; BAE77537; BAE77537.
DR GeneID; 948261; -.
DR KEGG; ecj:JW3730; -.
DR KEGG; eco:b3751; -.
DR PATRIC; fig|1411691.4.peg.2949; -.
DR EchoBASE; EB0808; -.
DR eggNOG; COG1879; Bacteria.
DR HOGENOM; CLU_037628_3_2_6; -.
DR InParanoid; P02925; -.
DR OMA; QAVFAHN; -.
DR PhylomeDB; P02925; -.
DR BioCyc; EcoCyc:RBSB-MON; -.
DR BioCyc; MetaCyc:RBSB-MON; -.
DR EvolutionaryTrace; P02925; -.
DR PRO; PR:P02925; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
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:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0048029; F:monosaccharide binding; IPI:EcoCyc.
DR GO; GO:0015752; P:D-ribose transmembrane transport; IDA:EcoCyc.
DR GO; GO:0050918; P:positive chemotaxis; IDA:EcoCyc.
DR InterPro; IPR028082; Peripla_BP_I.
DR InterPro; IPR025997; SBP_2_dom.
DR Pfam; PF13407; Peripla_BP_4; 1.
DR SUPFAM; SSF53822; SSF53822; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chemotaxis; Direct protein sequencing; Periplasm;
KW Reference proteome; Signal; Sugar transport; Transport.
FT SIGNAL 1..25
FT /evidence="ECO:0000269|PubMed:8899705,
FT ECO:0000269|PubMed:9298646"
FT CHAIN 26..296
FT /note="Ribose import binding protein RbsB"
FT /id="PRO_0000031732"
FT STRAND 28..34
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 39..55
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:2DRI"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:2DRI"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 97..105
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 110..115
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 130..145
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 150..155
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 161..177
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 180..186
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 191..204
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 210..215
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 216..229
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:2DRI"
FT HELIX 262..277
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:2DRI"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:2DRI"
SQ SEQUENCE 296 AA; 30950 MW; E5FA305A64EF3ACE CRC64;
MNMKKLATLV SAVALSATVS ANAMAKDTIA LVVSTLNNPF FVSLKDGAQK EADKLGYNLV
VLDSQNNPAK ELANVQDLTV RGTKILLINP TDSDAVGNAV KMANQANIPV ITLDRQATKG
EVVSHIASDN VLGGKIAGDY IAKKAGEGAK VIELQGIAGT SAARERGEGF QQAVAAHKFN
VLASQPADFD RIKGLNVMQN LLTAHPDVQA VFAQNDEMAL GALRALQTAG KSDVMVVGFD
GTPDGEKAVN DGKLAATIAQ LPDQIGAKGV ETADKVLKGE KVQAKYPVDL KLVVKQ
