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



Gene: livH Accession Numbers: EG10538 (EcoCyc), b3457, ECK3441

Synonyms: hrbD, hrbC, hrbB

Regulation Summary Diagram: ?

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

Gene Citations: [Adams90, Haney92]

Locations: inner membrane

Map Position: [3,593,500 <- 3,594,426] (77.45 centisomes)
Length: 927 bp / 308 aa

Molecular Weight of Polypeptide: 32.982 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0011290 , CGSC:552 , EchoBASE:EB0533 , EcoGene:EG10538 , EcoliWiki:b3457 , OU-Microarray:b3457 , PortEco:livH , PR:PRO_000023096 , Protein Model Portal:P0AEX7 , RefSeq:NP_417914 , RegulonDB:EG10538 , String:511145.b3457 , UniProt:P0AEX7

Relationship Links: InterPro:IN-FAMILY:IPR001851 , Pfam:IN-FAMILY:PF02653

In Paralogous Gene Group: 189 (15 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0015803 - branched-chain amino acid transport Inferred from experiment [Adams90]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a, GOA01a]
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:0005215 - transporter activity Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell structure membrane
metabolism biosynthesis of building blocks amino acids isoleucine/valine
metabolism biosynthesis of building blocks amino acids leucine
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, membrane component

Essentiality data for livH knockouts: ?

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

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


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


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 22 -> 42
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 46 -> 66
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 69 -> 89
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 105 -> 125
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 155 -> 175
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 204 -> 224
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 246 -> 266
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 253
[Nazos86, Adams90, UniProt10a]
Alternate sequence: S → G; UniProt: (in Ref. 1 and 2);
Transmembrane-Region 281 -> 301
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 288
[Nazos86, Adams90, UniProt10a]
Alternate sequence: L → P; UniProt: (in Ref. 1 and 2);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b3457 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10538; 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

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

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

Nazos86: Nazos PM, Antonucci TK, Landick R, Oxender DL (1986). "Cloning and characterization of livH, the structural gene encoding a component of the leucine transport system in Escherichia coli." J Bacteriol 166(2);565-73. PMID: 3009409

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

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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."

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, BIOCYC14A.