Escherichia coli K-12 substr. MG1655 Polypeptide: ribose ABC transporter - putative ATP binding subunit

Gene: rbsA Accession Numbers: EG10814 (EcoCyc), b3749, ECK3743

Synonyms: rbsT, rbsP

Regulation Summary Diagram

Regulation summary diagram for rbsA

Component of: ribose ABC transporter (extended summary available)

Gene Citations: [Bell86, Burland93]

Locations: inner membrane, cytosol

Map Position: [3,931,801 -> 3,933,306] (84.74 centisomes, 305°)
Length: 1506 bp / 501 aa

Molecular Weight of Polypeptide: 55.042 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0012259, CGSC:12082, DIP:DIP-10640N, EchoBASE:EB0807, EcoGene:EG10814, EcoliWiki:b3749, ModBase:P04983, OU-Microarray:b3749, PortEco:rbsA, PR:PRO_000023682, Pride:P04983, Protein Model Portal:P04983, RefSeq:NP_418205, RegulonDB:EG10814, SMR:P04983, String:511145.b3749, UniProt:P04983

Relationship Links: InterPro:IN-FAMILY:IPR003439, InterPro:IN-FAMILY:IPR003593, InterPro:IN-FAMILY:IPR015861, InterPro:IN-FAMILY:IPR017871, InterPro:IN-FAMILY:IPR027417, Pfam:IN-FAMILY:PF00005, Prosite:IN-FAMILY:PS00211, Prosite:IN-FAMILY:PS50893, Prosite:IN-FAMILY:PS51254, Smart:IN-FAMILY:SM00382

In Paralogous Gene Group: 23 (75 members)

Gene-Reaction Schematic

Gene-Reaction Schematic

Genetic Regulation Schematic

Genetic regulation schematic for rbsA

GO Terms:
Biological Process:
Inferred by computational analysisGO:0006810 - transport [UniProtGOA11a]
Inferred by computational analysisGO:0008152 - metabolic process [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0008643 - carbohydrate transport [UniProtGOA11a]
Inferred by computational analysisGO:0015752 - D-ribose transport [GOA06]
Inferred by computational analysisGO:0034219 - carbohydrate transmembrane transport [GOA01a]
Inferred by computational analysisGO:0042882 - L-arabinose transport [GOA01a]
Molecular Function:
Inferred from experimentGO:0005515 - protein binding [Rajagopala14]
Inferred by computational analysisGO:0000166 - nucleotide binding [UniProtGOA11a]
Inferred by computational analysisGO:0005524 - ATP binding [UniProtGOA11a, GOA06, GOA01a]
Inferred by computational analysisGO:0015407 - monosaccharide-transporting ATPase activity [GOA01]
Inferred by computational analysisGO:0015591 - D-ribose transmembrane transporter activity [GOA06]
Inferred by computational analysisGO:0015612 - L-arabinose-importing ATPase activity [GOA01a]
Inferred by computational analysisGO:0016787 - hydrolase activity [UniProtGOA11a]
Inferred by computational analysisGO:0016887 - ATPase activity [GOA01a]
Inferred by computational analysisGO:0043211 - carbohydrate-transporting ATPase activity [GOA01a]
Cellular Component:
GO:0005737 - cytoplasm []
GO:0005829 - cytosol []
Inferred by computational analysisGO:0005886 - plasma membrane [UniProtGOA11, UniProtGOA11a, DiazMejia09]
Inferred by computational analysisGO:0016020 - membrane [UniProtGOA11a, GOA01a]
Inferred by computational analysisGO:0043190 - ATP-binding cassette (ABC) transporter complex [GOA06]

MultiFun Terms: metabolismcarbon utilizationcarbon compounds
transportChannel-type TransportersPyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active TransportersThe ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake PermeasesABC superfamily ATP binding cytoplasmic component

Essentiality data for rbsA knockouts:

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB enrichedYes 37 Aerobic 6.95   Yes [Gerdes03, Comment 1]
LB LennoxYes 37 Aerobic 7   Yes [Baba06, Comment 2]
M9 medium with 1% glycerolYes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucoseYes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 2]
Yes [Feist07, Comment 4]

Subunit of: ribose ABC transporter

Subunit composition of ribose ABC transporter = [RbsA]2[RbsC]2[RbsB]
         ribose ABC transporter - putative ATP binding subunit = RbsA
         ribose ABC transporter - membrane subunit = RbsC
         ribose ABC transporter - putative periplasmic binding protein = RbsB

RbsACB is an ATP-dependent ribose transporter that is a member of the ATP-Binding Cassette (ABC) Superfamily of transporters [Park99]. Based on sequence similarity, RbsA is the ATP-binding constituent, RbsB is the periplasmic substrate-binding protein, and RbsC form the transmembrane constituent of the transporter [Park99]. Mutations in each of the components eliminated transport of ribose at external concentration of 1 μM, indicating that the components make up a transport system that is responsible for high-affinity ribose transport. However, these mutants are able to grow normally on high concentrations of the sugar, suggesting that there is at least a second, low-affinity transport system for ribose in E. coli [Iida84]. Hydrophobicity analysis has shown that RbsC contains six transmembrane helices, while alkaline phosphatase fusions and the use of inside-out vesicles with proteolysis have shown that the C and N termini are both on the cytoplasmic side of the membrane.

Enzymatic reaction of: transport of D-ribose (ribose ABC transporter)

Inferred from experimentInferred by computational analysis

EC Number:

Transport reaction diagram for transport of D-ribose

Sequence Features

Protein sequence of ribose ABC transporter - putative ATP binding subunit with features indicated

Feature Class Location Attached Group Citations Comment
Conserved-Region 5 -> 241  
Inferred by computational analysis[UniProt15]
UniProt: ABC transporter 1.
Pfam PF00005 22 -> 169  
Inferred by computational analysis[Finn14]
ABC_tran : ABC transporter
Nucleotide-Phosphate-Binding-Region 37 -> 44 ATP
Inferred by computational analysis[UniProt15]
UniProt: ATP.
Mutagenesis-Variant 43  
Inferred from experiment[Barroga96]
UniProt: Loss of transport.
Conserved-Region 252 -> 495  
Inferred by computational analysis[UniProt15]
UniProt: ABC transporter 2.
Pfam PF00005 269 -> 423  
Inferred by computational analysis[Finn14]
ABC_tran : ABC transporter

Gene Local Context (not to scale -- see Genome Browser for correct scale)

Gene local context diagram

Transcription Unit

Transcription-unit diagram


10/20/97 Gene b3749 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10814; confirmed by SwissProt match.


Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Barroga96: Barroga CF, Zhang H, Wajih N, Bouyer JH, Hermodson MA (1996). "The proteins encoded by the rbs operon of Escherichia coli: I. Overproduction, purification, characterization, and functional analysis of RbsA." Protein Sci 5(6);1093-9. PMID: 8762140

Bell86: Bell AW, Buckel SD, Groarke JM, Hope JN, Kingsley DH, Hermodson MA (1986). "The nucleotide sequences of the rbsD, rbsA, and rbsC genes of Escherichia coli K12." J Biol Chem 261(17);7652-8. PMID: 3011793

Burland93: Burland V, Plunkett G, Daniels DL, Blattner FR (1993). "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome: organizational symmetry around the origin of replication." Genomics 1993;16(3);551-61. PMID: 7686882

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

Finn14: Finn RD, Bateman A, Clements J, Coggill P, Eberhardt RY, Eddy SR, Heger A, Hetherington K, Holm L, Mistry J, Sonnhammer EL, Tate J, Punta M (2014). "Pfam: the protein families database." Nucleic Acids Res 42(Database issue);D222-30. PMID: 24288371

Gerdes03: Gerdes SY, Scholle MD, Campbell JW, Balazsi G, Ravasz E, Daugherty MD, Somera AL, Kyrpides NC, Anderson I, Gelfand MS, Bhattacharya A, Kapatral V, D'Souza M, Baev MV, Grechkin Y, Mseeh F, Fonstein MY, Overbeek R, Barabasi AL, Oltvai ZN, Osterman AL (2003). "Experimental determination and system level analysis of essential genes in Escherichia coli MG1655." J Bacteriol 185(19);5673-84. PMID: 13129938

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Iida84: Iida A, Harayama S, Iino T, Hazelbauer GL (1984). "Molecular cloning and characterization of genes required for ribose transport and utilization in Escherichia coli K-12." J Bacteriol 158(2);674-82. PMID: 6327617

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Park99: Park Y, Park C (1999). "Topology of RbsC, a membrane component of the ribose transporter, belonging to the AraH superfamily." J Bacteriol 1999;181(3);1039-42. PMID: 9922273

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

UniProt15: UniProt Consortium (2015). "UniProt version 2015-08 released on 2015-07-22." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Mauzy92: Mauzy CA, Hermodson MA (1992). "Structural and functional analyses of the repressor, RbsR, of the ribose operon of Escherichia coli." Protein Sci 1992;1(7);831-42. PMID: 1304369

Shimada13a: Shimada T, Kori A, Ishihama A (2013). "Involvement of the ribose operon repressor RbsR in regulation of purine nucleotide synthesis in Escherichia coli." FEMS Microbiol Lett 344(2);159-65. PMID: 23651393

Zheng04: Zheng D, Constantinidou C, Hobman JL, Minchin SD (2004). "Identification of the CRP regulon using in vitro and in vivo transcriptional profiling." Nucleic Acids Res 32(19);5874-93. PMID: 15520470

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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