(data stored in SCRATCH zone)

SWISSPROT: 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   11-DEC-2019, entry version 174.
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;
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;
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;
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;
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;
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;
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       P00956:ileS; NbExp=3; IntAct=EBI-369930, EBI-552928;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:1583688}.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 2 family.
CC       {ECO:0000305}.
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   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; 16.
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   EPD; 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; ENOG4105E9V; Bacteria.
DR   eggNOG; COG1879; LUCA.
DR   HOGENOM; HOG000212345; -.
DR   InParanoid; P02925; -.
DR   KO; K10439; -.
DR   PhylomeDB; P02925; -.
DR   BioCyc; EcoCyc:RBSB-MONOMER; -.
DR   BioCyc; ECOL316407:JW3730-MONOMER; -.
DR   BioCyc; MetaCyc:RBSB-MONOMER; -.
DR   EvolutionaryTrace; P02925; -.
DR   PRO; PR:P02925; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
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;
DR   PRODOM; P02925.
DR   SWISS-2DPAGE; P02925.
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:0000244|PDB:2DRI"
FT   STRAND          36..38
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           39..55
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          58..63
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           68..78
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   TURN            79..82
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          83..88
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   TURN            93..96
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           97..105
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          110..115
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          118..120
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          123..128
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           130..145
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          150..155
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           161..177
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          180..186
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           191..204
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          210..215
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           216..229
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          235..240
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           243..250
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          256..259
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   HELIX           262..277
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          284..288
FT                   /evidence="ECO:0000244|PDB:2DRI"
FT   STRAND          291..293
FT                   /evidence="ECO:0000244|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
//

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