Ribose import binding protein RbsB
Details
- Name
- Ribose import binding protein RbsB
- Kind
- protein
- Synonyms
- prlB
- rbsP
- Gene Name
- rbsB
- UniProtKB Entry
- P02925Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- 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
- Functionsmonosaccharide transmembrane transporter activityProcesseschemotaxis / monosaccharide transportComponentsintegral component of membrane / membrane / outer membrane-bounded periplasmic space / plasma membrane
- General Function
- Part of the ABC transporter complex RbsABC involved in ribose import. Binds ribose. Also serves as the primary chemoreceptor for chemotaxis.
- Specific Function
- monosaccharide binding
- Pfam Domain Function
- Peripla_BP_4 (PF13407)
- Signal Regions
- 1-25
- 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
Resource Link UniProtKB ID P02925 UniProtKB Entry Name RBSB_ECOLI GenBank Protein ID 147519 GenBank Gene ID K00511 PDB ID(s) 1BA2, 1DBP, 1DRJ, 1DRK, 1URP, 2DRI, 2GX6 KEGG ID ecj:JW3730 NCBI Gene ID 948261 - General References
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
- 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]
Associated Data
- Drug Relations
Drug Drug group Pharmacological action? Type Actions Details beta-D-Ribopyranose experimental unknown target Details