Ribose import binding protein RbsB

Details

Name
Ribose import binding protein RbsB
Synonyms
  • prlB
  • rbsP
Gene Name
rbsB
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011398|Ribose import binding protein RbsB
MNMKKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLV
VLDSQNNPAKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRQATKG
EVVSHIASDNVLGGKIAGDYIAKKAGEGAKVIELQGIAGTSAARERGEGFQQAVAAHKFN
VLASQPADFDRIKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSDVMVVGFD
GTPDGEKAVNDGKLAATIAQLPDQIGAKGVETADKVLKGEKVQAKYPVDLKLVVKQ
Number of residues
296
Molecular Weight
30950.265
Theoretical pI
7.76
GO Classification
Functions
monosaccharide transmembrane transporter activity
Processes
chemotaxis / monosaccharide transport
Components
integral component of membrane / membrane / outer membrane-bounded periplasmic space / plasma membrane
General Function
Monosaccharide transmembrane transporter activity
Specific Function
Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Periplasm
Gene sequence
>lcl|BSEQ0011399|Ribose import binding protein RbsB (rbsB)
ATGAACATGAAAAAACTGGCTACCCTGGTTTCCGCTGTTGCGCTAAGCGCCACCGTCAGT
GCGAATGCGATGGCAAAAGACACCATCGCGCTGGTGGTCTCCACGCTTAACAACCCGTTC
TTTGTATCGCTGAAAGATGGCGCGCAGAAAGAGGCGGATAAACTTGGCTATAACCTGGTG
GTGCTGGACTCCCAGAACAACCCGGCGAAAGAGCTGGCGAACGTGCAGGACTTAACCGTT
CGCGGCACAAAAATTCTGCTGATTAACCCGACCGACTCCGACGCAGTGGGTAATGCTGTG
AAGATGGCTAACCAGGCGAACATCCCGGTTATCACTCTTGACCGCCAGGCAACGAAAGGT
GAAGTGGTGAGCCACATTGCTTCTGATAACGTACTGGGCGGCAAAATCGCTGGTGATTAC
ATCGCGAAGAAAGCGGGTGAAGGTGCCAAAGTTATCGAGCTGCAAGGCATTGCTGGTACA
TCCGCAGCCCGTGAACGTGGCGAAGGCTTCCAGCAGGCCGTTGCTGCTCACAAGTTTAAT
GTTCTTGCCAGCCAGCCAGCAGATTTTGATCGCATTAAAGGTTTGAACGTAATGCAGAAC
CTGTTGACCGCTCATCCGGATGTTCAGGCTGTATTCGCGCAGAATGATGAAATGGCGCTG
GGCGCGCTGCGCGCACTGCAAACTGCCGGTAAATCGGATGTGATGGTCGTCGGATTTGAC
GGTACACCGGATGGCGAAAAAGCGGTGAATGATGGCAAACTAGCAGCGACTATCGCTCAG
CTACCCGATCAGATTGGCGCGAAAGGCGTCGAAACCGCAGATAAAGTGCTGAAAGGCGAG
AAAGTTCAGGCTAAGTATCCGGTTGATCTGAAACTGGTTGTTAAGCAGTAG
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP02925
UniProtKB Entry NameRBSB_ECOLI
GenBank Protein ID147519
GenBank Gene IDK00511
General References
  1. Groarke JM, Mahoney WC, Hope JN, Furlong CE, Robb FT, Zalkin H, Hermodson MA: The amino acid sequence of D-ribose-binding protein from Escherichia coli K12. J Biol Chem. 1983 Nov 10;258(21):12952-6. [Article]
  2. Burland V, Plunkett G 3rd, Daniels DL, Blattner FR: DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication. Genomics. 1993 Jun;16(3):551-61. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Bell AW, Buckel SD, Groarke JM, Hope JN, Kingsley DH, Hermodson MA: The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12. J Biol Chem. 1986 Jun 15;261(17):7652-8. [Article]
  6. Hope JN, Bell AW, Hermodson MA, Groarke JM: Ribokinase from Escherichia coli K12. Nucleotide sequence and overexpression of the rbsK gene and purification of ribokinase. J Biol Chem. 1986 Jun 15;261(17):7663-8. [Article]
  7. Gonzalez-Gil G, Bringmann P, Kahmann R: FIS is a regulator of metabolism in Escherichia coli. Mol Microbiol. 1996 Oct;22(1):21-9. [Article]
  8. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  9. Willis RC, Furlong CE: Purification and properties of a ribose-binding protein from Escherichia coli. J Biol Chem. 1974 Nov 10;249(21):6926-9. [Article]
  10. Iida A, Harayama S, Iino T, Hazelbauer GL: Molecular cloning and characterization of genes required for ribose transport and utilization in Escherichia coli K-12. J Bacteriol. 1984 May;158(2):674-82. [Article]
  11. VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
  12. Clifton MC, Simon MJ, Erramilli SK, Zhang H, Zaitseva J, Hermodson MA, Stauffacher CV: In vitro reassembly of the ribose ATP-binding cassette transporter reveals a distinct set of transport complexes. J Biol Chem. 2015 Feb 27;290(9):5555-65. doi: 10.1074/jbc.M114.621573. Epub 2014 Dec 22. [Article]
  13. Mowbray SL, Cole LB: 1.7 A X-ray structure of the periplasmic ribose receptor from Escherichia coli. J Mol Biol. 1992 May 5;225(1):155-75. [Article]
  14. Bjorkman AJ, Binnie RA, Zhang H, Cole LB, Hermodson MA, Mowbray SL: Probing protein-protein interactions. The ribose-binding protein in bacterial transport and chemotaxis. J Biol Chem. 1994 Dec 2;269(48):30206-11. [Article]
  15. Bjorkman AJ, Mowbray SL: Multiple open forms of ribose-binding protein trace the path of its conformational change. J Mol Biol. 1998 Jun 12;279(3):651-64. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB04286beta-D-RibopyranoseexperimentalunknownDetails