Search:   Search E.coli Proteins by Name Accession Num Gene name Pi Mw Function/Expression


Entry Information
Protein Name RbsB
Accession No P02925
Protein description D-ribose-binding periplasmic protein
pI/Mw (Da)
Theoretical Experimental
5.99/28474.47 6.85/30900
5.92/29066 (DIGE 4.5-6.5)
Protein function and expression Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis. Repressed in the presence of glucose, but induced in the physiological short-term adaptation to glucose-limitation.
Reference(s) Han, M. -J., S. S. Yoon, and S. Y. Lee. 2001. Proteome analysis of metabolically engineered Escherichia coli producing poly(3-hydroxybutyrate). J. Bacteriol. 183:301-308. (NCBI)

Lopez-Campistrous, A., P. Semchuk, L. Burke, T. Palmer-Stone, S. J. Brokx, G. Broderick, D. Bottorff, S. Bolch, J. H. Weiner, and M. J. Ellison. 2005. Localization, annotation & comparison of the Escherichia coli K-12 proteome under two states of growth. Mol. Cell. Proteomics 4:1205-1209. (NCBI)

Wick, L. M., M. Quadroni, and T. Egli. 2001. Short- and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose-limited growth conditions in continuous culture and vice versa. Environ. Microbiol. 3:588-599. (NCBI)

Yan, J. X., A. T. Devenish, R. Wait, T. Stone, S. Lewis, and S. Fowler. 2002. Fluorescence two-dimensional difference gel electrophoresis and mass spectrometry based proteomic analysis of Escherichia coli. Proteomics 2:1682-1698. (NCBI)

2D gels information
Map ID38
Reference(s)Champion, K. M., J. C. Nishihara, J. C. Joly, and D. Arnott. 2001. Similarity of the Escherichia coli proteome upon completion of different biopharmaceutical fermentation processes. Proteomics 1:1133-1148. (NCBI)
Protein function and expression(s)Map: A B
pI/Mw: 5.99/28474

A
2-DE profile of E. coli proteins at the end of anti-CD18 blank run fermentation.
B
2-DE analysis of E. coli proteins from Nutropin production fermentation.
Map ID68
Reference(s)Fountoulakis, M., and R. Gasser. 2003. Proteomic analysis of the cell envelope fraction of Escherichia coli. Amino Acids 24:19-41. (NCBI)
Protein function and expression(s)Map: A B B B CB CB
Spot: 10


A
The membrane proteins of the wild type strain.
B
The membrane proteins of the E. coli transformant producing recombinant human cytochrome P450 2E1 and cytochrome P450 reductase
CB
The membrane proteins of E. coli producing human cytochrome P450 2D6 were solubilized with 0.5% sodium cholate. Cholate was exchanged against 7 M urea, 2 M thiourea and 1% Triton X-100.
Map ID99
Reference(s)Han, M. -J., S. S. Yoon, and S. Y. Lee. 2001. Proteome analysis of metabolically engineered Escherichia coli producing poly(3-hydroxybutyrate). J. Bacteriol. 183:301-308. (NCBI)
Protein function and expression(s)Map: A B C D
Spot: 6
Functional category: Transport binding

A
Proteome expression profile of E. coli XL1-Blue grown in LB medium.
B
Proteome expression profile of E. coli XL1-Blue grown in LB medium plus 20 g/L of glucose.
C
Proteome expression profile of E. coli XL1-Blue (pJC4) grown in LB medium.
D
Proteome expression profile of E. coli XL1-Blue (pJC4) grown in LB medium plus 20 g/L of glucose.
Map ID311
Reference(s)Wick, L. M., M. Quadroni, and T. Egli. 2001. Short- and long-term changes in proteome composition and kinetic properties in a culture of Escherichia coli during transition from glucose-excess to glucose-limited growth conditions in continuous culture and vice versa. Environ. Microbiol. 3:588-599. (NCBI)
Protein function and expression(s)Map: A B
Spot: 11
Functional category: Sugar transport

A
Proteins expressed in a culture of E. coli K12 during growth under glucose-excess batch.
B
Proteins expressed in a culture of E. coli K12 during growth under glucose-limited continuous.
Swiss-Prot Database Reference

Entry information
Entry Name RBSB_ECOLI
Primary accession number P02925
Secondary accession numbers Q2M869 
Integrated into Swiss-Prot on 1986-07-21
Sequence was last modified on 1986-07-21 (Sequence version 1)
Annotations were last modified on 2006-07-25 (Entry version 77)
Name and origin of the protein
Protein name D-ribose-binding periplasmic protein precursor
Synonyms EC 3.6.3.17 D-ribose-binding periplasmic protein precursor
Gene name Name : rbsB
OrderedLocusName : b3751
SynonymName : prlB
SynonymName : rbsP
From Escherichia coli [TaxID:562] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia;
References
[1] NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.PubMed=6313683[NCBI, ExPASy, EBI, Israel, Japan]
Groarke J.M. , Mahoney W.C. , Hope J.N. , Furlong C.E. , Robb F.T. , Zalkin H. , Hermodson M.A. ,
"The amino acid sequence of D-ribose-binding protein from Escherichia coli K12."
J. Biol. Chem.258:12952-12956(1983) 
[2] NUCLEOTIDE SEQUENCE [GENOMIC DNA].
strain = K12

Mauzy C.A. ,
Submitted (1986-02) to the EMBL/GenBank/DDBJ databases 
[3] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
PubMed=7686882[NCBI, ExPASy, EBI, Israel, Japan]
Burland V.D. , Plunkett G. III , Daniels D.L. , Blattner F.R. ,
"DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication."
Genomics16:551-561(1993) 
[4] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / MG1655 / ATCC 47076
DOI=10.1126/science.277.5331.1453;PubMed=9278503[NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R. , Plunkett G. III , Bloch C.A. , Perna N.T. , Burland V. , Riley M. , Collado-Vides J. , Glasner J.D. , Rode C.K. , Mayhew G.F. , Gregor J. , Davis N.W. , Kirkpatrick H.A. , Goeden M.A. , Rose D.J. , Mau B. , Shao Y. ,
"The complete genome sequence of Escherichia coli K-12."
Science277:1453-1474(1997) 
[5] NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
strain = K12 / W3110 / ATCC 27325 / DSM 5911
DOI=10.1038/msb4100049;
Hayashi K. , Morooka N. , Yamamoto Y. , Fujita K. , Isono K. , Choi S. , Ohtsubo E. , Baba T. , Wanner B.L. , Mori H. , Horiuchi T. ,
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Mol. Syst. Biol.2:E1-E5(2006) 
[6] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12.
strain = K12
PubMed=3011793[NCBI, ExPASy, EBI, Israel, Japan]
Bell A.W. , Buckel S.D. , Groarke J.M. , Hope J.N. , Kingsley D.H. , Hermodson M.A. ,
"The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12."
J. Biol. Chem.261:7652-7658(1986) 
[7] NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-296.
strain = K12
PubMed=3011794[NCBI, ExPASy, EBI, Israel, Japan]
Hope J.N. , Bell A.W. , Hermodson M.A. , Groarke J.M. ,
"Ribokinase from Escherichia coli K12. Nucleotide sequence and overexpression of the rbsK gene and purification of ribokinase."
J. Biol. Chem.261:7663-7668(1986) 
[8] PROTEIN SEQUENCE OF 26-39.
strain = K12
PubMed=8899705[NCBI, ExPASy, EBI, Israel, Japan]
Gonzalez-Gil G. , Bringmann P. , Kahmann R. ,
"FIS is a regulator of metabolism in Escherichia coli."
Mol. Microbiol.22:21-29(1996) 
[9] PROTEIN SEQUENCE OF 26-37.
strain = K12 / EMG2
PubMed=9298646[NCBI, ExPASy, EBI, Israel, Japan]
Link A.J. , Robison K. , Church G.M. ,
"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
Electrophoresis18:1259-1313(1997) 
[10] X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).PubMed=1583688[NCBI, ExPASy, EBI, Israel, Japan]
Mowbray S.L. , Cole L.B. ,
"1.7-A X-ray structure of the periplasmic ribose receptor from Escherichia coli."
J. Mol. Biol.225:155-175(1992) 
[11] X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).PubMed=7982928[NCBI, ExPASy, EBI, Israel, Japan]
Bjoerkman A.J. , Binnie R.A. , Zhang H. , Cole L.B. , Hermodson M.A. , Mowbray S.L. ,
"Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis."
J. Biol. Chem.269:30206-30211(1994) 
[12] X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).DOI=10.1006/jmbi.1998.1785;PubMed=9641984[NCBI, ExPASy, EBI, Israel, Japan]
Bjoerkman A.J. , Mowbray S.L. ,
"Multiple open forms of ribose-binding protein trace the path of its conformational change."
J. Mol. Biol.279:651-664(1998) 
Comments
  • FUNCTION : Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis
  • CATALYTIC ACTIVITY : ATP + H(2)O + monosaccharide(Out) = ADP + phosphate + monosaccharide(In)
  • SUBCELLULAR LOCATION : Periplasm
  • SIMILARITY : Belongs to the bacterial solute-binding protein 2 family
    • Copyright
    Copyrighted by the UniProt Consortium, see http://www.uniprot.org/. Distributed under the Creative Commons Attribution-NoDerivs License.
    Cross-reference
    Sequence databases
    EMBL K00511;AAA50966.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    M13169;AAA51475.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    L10328;AAA62104.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    U00096;AAC76774.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    AP009048;BAE77537.1;-;Genomic_DNA [EMBL/GenBank/DDBJ][CoDingSequence].
    PIR A03425;JGECR.
    3D structure databases
    PDB 1BA2;X-ray;A/B=26-296[ExPASy/RCSB/EBI].
    1DBP;X-ray;@=26-296[ExPASy/RCSB/EBI].
    1DRJ;X-ray;@=26-296[ExPASy/RCSB/EBI].
    1DRK;X-ray;@=26-296[ExPASy/RCSB/EBI].
    1URP;X-ray;A/B/C/D=26-296[ExPASy/RCSB/EBI].
    2DRI;X-ray;@=26-296[ExPASy/RCSB/EBI].
    Detailed list of linked structures
    ModBase P02925
    Protein-protein interaction databases
    IntAct P02925;-.
    DIP P02925
    Enzyme and pathway databases
    BioCyc EcoCyc:RBSB-MONOMER;-.
    2D gel databases
    SWISS-2DPAGE P02925;COLI.
    Organism-specific gene databases
    EchoBASE EB0808;-.
    ECO2DBASE H027.9;6TH EDITION.
    EcoGene EG10815;rbsB.
    HOGENOM [Family / Alignment / Tree]
    Family and domain databases
    InterPro IPR001761;Peripla_BP_Lac1.
    Graphical view of domain structure
    Pfam PF00532;Peripla_BP_1;1.
    Pfam graphical view of domain structure
    BLOCKS P02925
    Genome annotation databases
    GenomeReviews U00096_GR;b3751.
    Other
    LinkHub P02925;-.
    ProtoNet P02925
    UniRef View cluster of proteins with at least 50% / 90% / 100% identity
    Keyword
    3D-structure; Chemotaxis; Complete proteome; Direct protein sequencing; Hydrolase; Periplasmic; Signal; Sugar transport; Transport;
    Features
    Feature table viewer Feature aligner
    Key  From   To Length  Description  FTId
    SIGNAL    1    25     25    
    CHAIN   26   296    271  D-ribose-binding periplasmic protein  PRO_0000031732
    STRAND   28    34      7    
    STRAND   36    38      3    
    HELIX   39    55     17    
    TURN   56    56      1    
    STRAND   58    63      6    
    TURN   65    66      2    
    HELIX   68    78     11    
    TURN   79    82      4    
    STRAND   83    88      6    
    STRAND   91    92      2    
    TURN   93    96      4    
    HELIX   97   105      9    
    TURN  106   107      2    
    STRAND  110   115      6    
    STRAND  118   120      3    
    STRAND  123   128      6    
    HELIX  130   145     16    
    TURN  147   148      2    
    STRAND  150   155      6    
    TURN  158   159      2    
    HELIX  161   177     17    
    TURN  178   178      1    
    STRAND  180   186      7    
    TURN  188   189      2    
    HELIX  191   204     14    
    TURN  206   207      2    
    STRAND  210   215      6    
    HELIX  216   229     14    
    TURN  230   230      1    
    STRAND  233   233      1    
    STRAND  235   240      6    
    HELIX  243   250      8    
    TURN  251   252      2    
    STRAND  253   254      2    
    STRAND  256   259      4    
    HELIX  262   277     16    
    TURN  278   279      2    
    STRAND  284   288      5    
    STRAND  291   293      3    
    Sequence information
    Length: 296AA [This is the length of the unprocessed precursor] Molecular weight: 30950Da [This is the MW of the unprocessed precursor] CRC64: E5FA305A64EF3ACE[This is a checksum on the sequence] 
            10         20         30         40         50         60
MNMKKLATLV SAVALSATVS ANAMAKDTIA LVVSTLNNPF FVSLKDGAQK EADKLGYNLV
        70         80         90        100        110        120
VLDSQNNPAK ELANVQDLTV RGTKILLINP TDSDAVGNAV KMANQANIPV ITLDRQATKG
       130        140        150        160        170        180
EVVSHIASDN VLGGKIAGDY IAKKAGEGAK VIELQGIAGT SAARERGEGF QQAVAAHKFN
       190        200        210        220        230        240
VLASQPADFD RIKGLNVMQN LLTAHPDVQA VFAQNDEMAL GALRALQTAG KSDVMVVGFD
       250        260        270        280        290 
GTPDGEKAVN DGKLAATIAQ LPDQIGAKGV ETADKVLKGE KVQAKYPVDL KLVVKQ
    		 P02925 in FASTA format

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