D-ribose-binding periplasmic protein (P02925)

Identification
Name:D-ribose-binding periplasmic protein
Synonyms:Not Available
Gene Name:rbsB
Enzyme Class:Not Available
Biological Properties
General Function:Carbohydrate transport and metabolism
Specific Function:Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis
Cellular Location:Periplasm
SMPDB Pathways:
KEGG Pathways:
SMPDB Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0beta-D-Ribopyranose + 1.0Adenosine triphosphate + 1.0Water → 1.0ADP + 1.0Phosphate + 1.0Hydrogen ion
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Ribose → 1.0ADP + 1.0Hydrogen ion + 1.0Phosphate + 1.0Ribose
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB01341ADPMetaboCard
ECMDB20344beta-D-RibopyranoseMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00283RiboseMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:Not Available
Gene Properties
Blattner:b3751
Gene OrientationClockwise
Centisome Percentage:84.80
Left Sequence End3934301
Right Sequence End3935191
Gene Sequence:
>891 bp
ATGAGCGGCTTACCTCTTATTTCGCGCCGTCGACTGTTAACGGCGATGGCGCTTTCTCCG
TTGTTATGGCAGATGAATACCGCCCACGCGGCGGCTATTGATCCCAATCGTATTGTGGCG
CTGGAGTGGTTGCCGGTGGAATTACTGCTGGCGCTCGGCATCGTGCCTTACGGCGTGGCG
GATACCATCAACTATCGCCTGTGGGTCAGCGAACCACCATTGCCGGACTCAGTGATCGAC
GTCGGTTTGCGCACAGAACCTAACCTTGAACTGCTGACCGAAATGAAACCATCGTTTATG
GTCTGGTCGGCAGGATATGGCCCTTCACCAGAAATGCTGGCTCGTATTGCGCCGGGTCGC
GGATTTAACTTCAGTGACGGCAAACAGCCGTTGGCGATGGCGCGTAAATCGCTGACGGAA
ATGGCAGATTTACTTAACCTGCAAAGCGCAGCGGAAACGCATTTAGCGCAATATGAAGAC
TTTATCCGCAGCATGAAACCCCGCTTTGTGAAGCGTGGTGCGCGTCCGTTATTGCTGACG
ACGCTTATCGATCCGCGCCATATGCTGGTCTTCGGTCCAAACAGCTTGTTCCAGGAAATT
CTTGATGAGTACGGCATCCCAAATGCCTGGCAAGGGGAAACCAACTTCTGGGGCAGTACC
GCCGTCAGTATCGATCGTCTGGCGGCGTATAAAGACGTTGATGTGCTCTGTTTTGATCAC
GACAACAGCAAAGACATGGATGCGCTAATGGCAACGCCGCTGTGGCAGGCCATGCCGTTT
GTCCGCGCCGGACGCTTTCAGCGCGTACCTGCAGTCTGGTTTTATGGTGCGACGCTCTCG
GCAATGCACTTTGTGCGCGTTCTGGATAACGCCATCGGAGGTAAAGCGTGA
Protein Properties
Pfam Domain Function:
Protein Residues:296
Protein Molecular Weight:30950
Protein Theoretical pI:8
PDB File:1URP
Signaling Regions:
  • 1-25
Transmembrane Regions:
  • None
Protein Sequence:
>D-ribose-binding periplasmic protein
MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLV
VLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKG
EVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFN
VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD
GTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
References
External Links:
ResourceLink
Uniprot ID:P02925
Uniprot Name:RBSB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674358
PDB ID:1URP
Ecogene ID:EG10815
Ecocyc:EG10815
ColiBase:b3751
Kegg Gene:b3751
EchoBASE ID:EB0808
CCDB:RBSB_ECOLI
BacMap:16131619
General Reference:
  • Bell, A. W., Buckel, S. D., Groarke, J. M., Hope, J. N., Kingsley, D. H., Hermodson, M. A. (1986). "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12." J Biol Chem 261:7652-7658. Pubmed: 3011793
  • Bjorkman, A. J., Binnie, R. A., Zhang, H., Cole, L. B., Hermodson, M. A., Mowbray, S. L. (1994). "Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis." J Biol Chem 269:30206-30211. Pubmed: 7982928
  • Bjorkman, A. J., Mowbray, S. L. (1998). "Multiple open forms of ribose-binding protein trace the path of its conformational change." J Mol Biol 279:651-664. Pubmed: 9641984
  • Blattner, F. R., Plunkett, G. 3rd, 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. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Daniels, D. L., Blattner, F. R. (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 16:551-561. Pubmed: 7686882
  • Gonzalez-Gil, G., Bringmann, P., Kahmann, R. (1996). "FIS is a regulator of metabolism in Escherichia coli." Mol Microbiol 22:21-29. Pubmed: 8899705
  • Groarke, J. M., Mahoney, W. C., Hope, J. N., Furlong, C. E., Robb, F. T., Zalkin, H., Hermodson, M. A. (1983). "The amino acid sequence of D-ribose-binding protein from Escherichia coli K12." J Biol Chem 258:12952-12956. Pubmed: 6313683
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hope, J. N., Bell, A. W., Hermodson, M. A., Groarke, J. M. (1986). "Ribokinase from Escherichia coli K12. Nucleotide sequence and overexpression of the rbsK gene and purification of ribokinase." J Biol Chem 261:7663-7668. Pubmed: 3011794
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Mowbray, S. L., Cole, L. B. (1992). "1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli." J Mol Biol 225:155-175. Pubmed: 1583688