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Escherichia coli K-12 substr. MG1655 Polypeptide: branched chain amino acid ABC transporter - ATP binding subunit



Gene: livF Accession Numbers: EG10536 (EcoCyc), b3454, ECK3438

Regulation Summary Diagram: ?

Component of:
branched chain amino acid ABC transporter (extended summary available)
leucine ABC transporter (extended summary available)

Gene Citations: [Adams90, Haney92]

Locations: inner membrane

Map Position: [3,590,747 <- 3,591,460] (77.39 centisomes)
Length: 714 bp / 237 aa

Molecular Weight of Polypeptide: 26.31 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0011282 , CGSC:33713 , EchoBASE:EB0531 , EcoGene:EG10536 , EcoliWiki:b3454 , ModBase:P22731 , OU-Microarray:b3454 , PortEco:livF , PR:PRO_000023094 , Pride:P22731 , Protein Model Portal:P22731 , RefSeq:NP_417911 , RegulonDB:EG10536 , SMR:P22731 , String:511145.b3454 , Swiss-Model:P22731 , UniProt:P22731

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

In Paralogous Gene Group: 23 (75 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006812 - cation transport Inferred from experiment [Adams90]
GO:0015803 - branched-chain amino acid transport Inferred from experiment [Adams90]
GO:0015804 - neutral amino acid transport Inferred from experiment [Adams90]
GO:0015807 - L-amino acid transport Inferred from experiment [Adams90]
GO:0098655 - cation transmembrane transport Inferred from experiment [Adams90]
GO:1902475 - L-alpha-amino acid transmembrane transport Inferred from experiment [Adams90]
GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006865 - amino acid transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0015658 - branched-chain amino acid transmembrane transporter activity Inferred from experiment [Adams90]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids isoleucine/valine
metabolism biosynthesis of building blocks amino acids leucine
metabolism carbon utilization amino acids
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 ATP binding cytoplasmic component

Essentiality data for livF 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: branched chain amino acid ABC transporter

Subunit composition of branched chain amino acid ABC transporter = [LivF][LivG][LivH][LivM][LivJ]
         branched chain amino acid ABC transporter - ATP binding subunit = LivF
         branched chain amino acid transporter - ATP binding subunit = LivG
         branched chain amino acid transporter - membrane subunit = LivH
         branched chain amino acid transporter - membrane subunit = LivM
         branched chain amino acid ABC transporter - periplasmic binding protein = LivJ

Summary:
LivFGHMJ and LivFGHMK are two ATP-dependent high-affinity branched-chain amino acid transport systems and are members of the ATP Binding Cassette (ABC) Superfamily of transporters [Igarashi99].

The two systems are responsible for the high affinity transport of branched-chain amino acids in E. coli. They have shared membrane and ATP-binding components but have distinctive periplasmic binding proteins. Due to the different periplasmic binding components, the two complexes differ in their binding specificity: LivFGHMK is specific for the transport of leucine, while LivFGHMJ is a transporter for leucine, isoleucine and valine [Nazos85].

Based on sequence similarity and hydrophobicity analysis, LivJ and LivK are the two periplasmic animo acid-binding proteins, LivH and LivM are the membrane components, and LivG and LivF are the ATP-binding component of the ABC transport complexes [Adams90].

Deletion of each of the liv genes resulted in the inability to transport leucine [Adams90]. In addition, a deletion strain that does not express any of the liv genes was unable to carry out high-affinity transport of leucine unless one of the binding protein genes and all of the membrane complex genes were provided on a plasmid [Adams90]. In a separate experiment, liv gene mutants were found to be resistant to a toxic analog of leucine, azaleucine, due to its inability in branched-chain amino acid transport [Nazos85]. This system has also been shown [Koyanagi04] to serve as a third (along with the AroP and PheP systems) complex for transport of phenylanine across the inner membrane.


Enzymatic reaction of: transport of L-leucine (branched chain amino acid ABC transporter)

Synonyms: Transport of L-leucine

Alternative Products for L-leucine: L-threonine [Landick85 ] , L-alanine [Landick85 ]


Enzymatic reaction of: transport of L-valine (branched chain amino acid ABC transporter)

Synonyms: Transport of L-valine


Enzymatic reaction of: transport of L-isoleucine (branched chain amino acid ABC transporter)

Synonyms: Transport of L-isoleucine


Subunit of: leucine ABC transporter

Subunit composition of leucine ABC transporter = [LivK][LivM][LivH][LivG][LivF]
         leucine ABC transporter - periplasmic binding protein = LivK (summary available)
         branched chain amino acid transporter - membrane subunit = LivM
         branched chain amino acid transporter - membrane subunit = LivH
         branched chain amino acid transporter - ATP binding subunit = LivG
         branched chain amino acid ABC transporter - ATP binding subunit = LivF

Summary:
LivFGHMJ and LivFGHMK are two ATP-dependent high-affinity branched-chain amino acid transport system and are members of the ATP Binding Cassette (ABC) Superfamily of transporters [Igarashi99]. The two systems are responsible for the high affinity transport of branched-chain amino acids in E. coli. They have shared membrane and ATP-binding components but have distinctive periplasmic binding proteins. Due to the different periplasmic binding components, the two complexes differ in their binding specificity: LivFGHMK is specific for the transport of leucine, while LivFGHMJ is a transporter for leucine, isoleucine, and valine [Nazos85]. Based on sequence similarity and hydrophobicity analysis, LivJ and LivK are the two periplasmic animo acid-binding proteins, LivH and LivM are the membrane components, and LivG and LivF are the ATP-binding component of the ABC transport complexes [Adams90]. Deletions each of the liv genes resulted in the inability to transport leucine [Adams90]. In addition, a deletion strain that does not express any of the liv genes was unable to carry out high-affinity transport of leucine unless one of the binding protein genes and all of the membrane complex genes were provided on a plasmid [Adams90]. In a separate experiment, liv gene mutants were found to be resistant to a toxic analog of leucine, azaleucine, due to its inability in branched-chain amino acid transport [Nazos85].


Enzymatic reaction of: leucine transporter (leucine ABC transporter)

Synonyms: Transport of L-leucine


Sequence Features

Feature Class Location Citations Comment
Conserved-Region 6 -> 237
[UniProt09]
UniProt: ABC transporter;
Nucleotide-Phosphate-Binding-Region 38 -> 45
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 56
[Adams90, UniProt10]
Alternate sequence: R → G; UniProt: (in Ref. 1; AAA83887);
Sequence-Conflict 120
[Adams90, UniProt10]
Alternate sequence: V → A; UniProt: (in Ref. 1; AAA83887);
Sequence-Conflict 200
[Adams90, UniProt10]
Alternate sequence: A → G; UniProt: (in Ref. 1; AAA83887);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene right-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
10/20/97 Gene b3454 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10536; confirmed by SwissProt match.


References

Adams90: Adams MD, Wagner LM, Graddis TJ, Landick R, Antonucci TK, Gibson AL, Oxender DL (1990). "Nucleotide sequence and genetic characterization reveal six essential genes for the LIV-I and LS transport systems of Escherichia coli." J Biol Chem 1990;265(20);11436-43. PMID: 2195019

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

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

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."

Haney92: Haney SA, Platko JV, Oxender DL, Calvo JM (1992). "Lrp, a leucine-responsive protein, regulates branched-chain amino acid transport genes in Escherichia coli." J Bacteriol 1992;174(1);108-15. PMID: 1729203

Igarashi99: Igarashi K, Kashiwagi K (1999). "Polyamine transport in bacteria and yeast." Biochem J 1999;344 Pt 3;633-42. PMID: 10585849

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

Koyanagi04: Koyanagi T, Katayama T, Suzuki H, Kumagai H (2004). "Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12." J Bacteriol 186(2);343-50. PMID: 14702302

Landick85: Landick R, Oxender DL (1985). "The complete nucleotide sequences of the Escherichia coli LIV-BP and LS-BP genes. Implications for the mechanism of high-affinity branched-chain amino acid transport." J Biol Chem 260(14);8257-61. PMID: 3891753

Nazos85: Nazos PM, Mayo MM, Su TZ, Anderson JJ, Oxender DL (1985). "Identification of livG, a membrane-associated component of the branched-chain amino acid transport in Escherichia coli." J Bacteriol 1985;163(3);1196-202. PMID: 2993238

Penrose68: Penrose WR, Nichoalds GE, Piperno JR, Oxender DL (1968). "Purification and properties of a leucine-binding protein from Escherichia coli." J Biol Chem 243(22);5921-8. PMID: 4972226

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

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.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

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

Wood75: Wood JM (1975). "Leucine transport in Escherichia coli. The resolution of multiple transport systems and their coupling to metabolic energy." J Biol Chem 250(12);4477-85. PMID: 1095572

Other References Related to Gene Regulation

Landick80: Landick R, Anderson JJ, Mayo MM, Gunsalus RP, Mavromara P, Daniels CJ, Oxender DL (1980). "Regulation of high-affinity leucine transport in Escherichia coli." J Supramol Struct 1980;14(4);527-37. PMID: 7017282


Report Errors or Provide Feedback
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 18.5 on Thu Nov 27, 2014, biocyc13.