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Escherichia coli K-12 substr. MG1655 Polypeptide: taurine ABC transporter - periplasmic binding protein

Gene: tauA Accession Numbers: G6217 (EcoCyc), b0365, ECK0362

Synonyms: yaiR, ssiA, taurine transport system periplasmic protein

Regulation Summary Diagram: ?

Regulation summary diagram for tauA

Component of: taurine ABC transporter (extended summary available)

TauA is the periplasmic substrate-binding component of the taurine ABC transporter.

Gene Citations: [vanderPloeg96, Kwon05]

Locations: periplasmic space

Map Position: [384,456 -> 385,418] (8.29 centisomes, 30°)
Length: 963 bp / 320 aa

Molecular Weight of Polypeptide: 34.266 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0001256 , EchoBASE:EB3085 , EcoGene:EG13300 , EcoliWiki:b0365 , ModBase:Q47537 , OU-Microarray:b0365 , PortEco:tauA , PR:PRO_000024033 , Pride:Q47537 , Protein Model Portal:Q47537 , RefSeq:NP_414899 , RegulonDB:G6217 , SMR:Q47537 , String:511145.b0365 , UniProt:Q47537

Relationship Links: InterPro:IN-FAMILY:IPR001638 , InterPro:IN-FAMILY:IPR007210 , InterPro:IN-FAMILY:IPR010068 , Pfam:IN-FAMILY:PF04069 , Smart:IN-FAMILY:SM00062

In Paralogous Gene Group: 227 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for tauA

GO Terms:

Biological Process: GO:0009970 - cellular response to sulfate starvation Inferred from experiment [vanderPloeg96]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0015734 - taurine transport Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005215 - transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred by computational analysis [DiazMejia09]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01a]

MultiFun Terms: metabolism carbon utilization amines
metabolism metabolism of other compounds sulfur metabolism
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, periplasmic binding component

Essentiality data for tauA knockouts: ?

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

Subunit of: taurine ABC transporter

Synonyms: TauA/TauB/TauC ABC transporter

Subunit composition of taurine ABC transporter = [TauA][TauC]2[TauB]2
         taurine ABC transporter - periplasmic binding protein = TauA (summary available)
         taurine ABC transporter - membrane subunit = TauC (summary available)
         taurine ABC transporter - ATP binding subunit = TauB (summary available)

The TauABC transporter belongs to the ATP Binding Cassette (ABC) superfamily [Wu95], and is believed to be responsible for taurine uptake in E. coli [vanderPloeg96]. E. coli rely on organosulfur compounds such as taurine as sources of sulfur when the level of inorganic sulfate available in the invironment is low [vanderPloeg96]. Disruption of the tauABC genes resulted in the loss of the ability to utilize taurine (2-aminoethanesulfonate) as a source of sulfur but did not affect the utilization of a range of other aliphatic sulfonates as sulfur sources. Taurine utilization was restored when the tauABC mutants were complemented with a clone of the tauABC locus [vanderPloeg96]. TauA contains a N-terminal signal sequence, indicating that it is probably located in the periplasm, and therefore may function as the substrate binding component of the ABC transporter [vanderPloeg96]. TauC is the membrane component of the TauABC taurine ABC transporter [vanderPloeg96]. Membrane topology predictions using experimentally determined C terminus locations indicate that TauC has 6 transmembrane helices and the C-terminus is located in the cytoplasm [Rapp04]. TauB and TauC show strong sequence similarities to ATP-binding components and membrane components, respectively, of other members of the ABC superfamily [vanderPloeg96]. Expression of tauABC is induced by sulfate starvation, and analysis of LacZ fusions showed that the tauABC operon is repressed by the presence of sulfur containing compounds, such as sulfate, cysteine, cystine, ethanesulfonate, and lanthionine [vanderPloeg96].

Deletions of tau transporter genes resulted in loss of the ability to utilize taurine, 3-aminopropanesulfonate, octanesulfonate, and decanesulfonate [Eichhorn00]. Deletions of tau transporter genes in addition to ssu transporter genes resulted in loss of ability to utilize PIPES, 2-(4-pyridyl)ethanesulfonate, isethionate, 1,3-dioxo-isoindolineethansulfonate, 3-aminopropanesulfonate, butanesulfonate and pentanesulfonate [Eichhorn00].

Enzymatic reaction of: taurine ABC transporter

Synonyms: transport of taurine

EC Number:

Transport reaction diagram for taurine ABC transporter

Sequence Features

Protein sequence of taurine ABC transporter - periplasmic binding protein with features indicated

Feature Class Location Citations Comment
Signal-Sequence 1 -> 22
Chain 23 -> 320
UniProt: Taurine-binding periplasmic protein;
Sequence-Conflict 62 -> 63
[Quadroni96, UniProt10]
UniProt: (in Ref. 5; AA sequence);
Sequence-Conflict 66
[Quadroni96, UniProt10]
UniProt: (in Ref. 5; AA sequence);
Sequence-Conflict 312
[Quadroni96, UniProt10]
UniProt: (in Ref. 5; AA sequence);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


Socorro Gama-Castro on Fri Oct 29, 2004:
The start site of this gene was originally assigned solely on the basis of sequence considerations [Blattner97 ]. However, it was changed because Van der Ploeg et al [vanderPloeg96 ] attested that the real start site is actually located 57 bp downstream. The demonstration is based on identification of both a plausible ribosome binding site and a promoter at an appropriate distance from the new start site. The promoter was identified using primer extension analysis.
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

Blattner97: Blattner FR, Plunkett G, 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 (1997). "The complete genome sequence of Escherichia coli K-12." Science 277(5331);1453-74. PMID: 9278503

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

Eichhorn00: Eichhorn E, van der Ploeg JR, Leisinger T (2000). "Deletion analysis of the Escherichia coli taurine and alkanesulfonate transport systems." J Bacteriol 182(10);2687-95. PMID: 10781534

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

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

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

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

Kwon05: Kwon O, Druce-Hoffman M, Meganathan R (2005). "Regulation of the Ubiquinone (Coenzyme Q) Biosynthetic Genes ubiCA in Escherichia coli." Curr Microbiol 50(4);180-9. PMID: 15902464

Quadroni96: Quadroni M, Staudenmann W, Kertesz M, James P (1996). "Analysis of global responses by protein and peptide fingerprinting of proteins isolated by two-dimensional gel electrophoresis. Application to the sulfate-starvation response of Escherichia coli." Eur J Biochem 239(3);773-81. PMID: 8774726

Rapp04: Rapp M, Drew D, Daley DO, Nilsson J, Carvalho T, Melen K, De Gier JW, Von Heijne G (2004). "Experimentally based topology models for E. coli inner membrane proteins." Protein Sci 13(4);937-45. PMID: 15044727

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

UniProt10: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 00:00:00." Database.

UniProt15: UniProt Consortium (2015). "UniProt version 2015-01 released on 2015-01-16 00:00:00." 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."

vanderPloeg96: van der Ploeg JR, Weiss MA, Saller E, Nashimoto H, Saito N, Kertesz MA, Leisinger T (1996). "Identification of sulfate starvation-regulated genes in Escherichia coli: a gene cluster involved in the utilization of taurine as a sulfur source." J Bacteriol 1996;178(18);5438-46. PMID: 8808933

Wu95: Wu LF, Mandrand-Berthelot MA (1995). "A family of homologous substrate-binding proteins with a broad range of substrate specificity and dissimilar biological functions." Biochimie 1995;77(9);744-50. PMID: 8789466

Other References Related to Gene Regulation

vanderPloeg97: van der Ploeg JR, Iwanicka-Nowicka R, Kertesz MA, Leisinger T, Hryniewicz MM (1997). "Involvement of CysB and Cbl regulatory proteins in expression of the tauABCD operon and other sulfate starvation-inducible genes in Escherichia coli." J Bacteriol 179(24);7671-8. PMID: 9401024

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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 19.0 on Sat Sep 5, 2015, biocyc12.