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



Gene: livK Accession Numbers: EG10540 (EcoCyc), b3458, ECK3442

Synonyms: hrbD, hrbC, hrbB

Regulation Summary Diagram: ?

Component of: leucine ABC transporter (extended summary available)

Summary:
The crystal structure of LivK in both the apo- and ligand-bound form has been determined at 1.5 and 1.8 A resolution [Sack89, Magnusson04a].

Gene Citations: [Adams90, Haney92]

Locations: periplasmic space

Map Position: [3,594,474 <- 3,595,583] (77.47 centisomes)
Length: 1110 bp / 369 aa

Molecular Weight of Polypeptide: 39.379 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0011292 , CGSC:550 , EchoBASE:EB0535 , EcoGene:EG10540 , EcoliWiki:b3458 , ModBase:P04816 , OU-Microarray:b3458 , PortEco:livK , PR:PRO_000023098 , Pride:P04816 , Protein Model Portal:P04816 , RefSeq:NP_417915 , RegulonDB:EG10540 , SMR:P04816 , String:511145.b3458 , UniProt:P04816

Relationship Links: InterPro:IN-FAMILY:IPR000709 , InterPro:IN-FAMILY:IPR028081 , InterPro:IN-FAMILY:IPR028082 , Panther:IN-FAMILY:PTHR30483 , PDB:Structure:1USG , PDB:Structure:1USI , PDB:Structure:1USK , PDB:Structure:2LBP , Pfam:IN-FAMILY:PF01094 , Pfam:IN-FAMILY:PF13458 , Prints:IN-FAMILY:PR00337

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0015807 - L-amino acid transport Inferred from experiment [Adams90]
GO:0015820 - leucine 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:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0006865 - amino acid transport Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0015190 - L-leucine transmembrane transporter activity Inferred from experiment [Adams90]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [GOA01, DiazMejia09, LopezCampistrou05]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11a, UniProtGOA11]

MultiFun Terms: 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, periplasmic binding component

Essentiality data for livK 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: 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
Signal-Sequence 1 -> 23
[Link97, UniProt11]
.
Sequence-Conflict 3
[Oxender80, UniProt10]
Alternate sequence: R → A; UniProt: (in Ref. 7; CAA23579);
Chain 24 -> 369
[UniProt09]
UniProt: Leucine-specific-binding protein;
Sequence-Conflict 43
[Adams90, Antonucci85, Landick85a, UniProt10]
Alternate sequence: D → I; UniProt: (in Ref. 1, 2 and 3);
Sequence-Conflict 50
[Adams90, Antonucci85, Landick85a, UniProt10]
Alternate sequence: R → E; UniProt: (in Ref. 1, 2 and 3);
Disulfide-Bond-Site 101, 76
[UniProt10a]
UniProt: Non-Experimental Qualifier: by similarity;
Sequence-Conflict 126
[Adams90, Antonucci85, Landick85a, UniProt10]
Alternate sequence: N → A; UniProt: (in Ref. 1, 2 and 3);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b3458 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10540; 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

Antonucci85: Antonucci TK, Landick R, Oxender DL (1985). "The leucine binding proteins of Escherichia coli as models for studying the relationships between protein structure and function." J Cell Biochem 29(3);209-16. PMID: 4077929

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

GOA01: 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

Landick85a: 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

Link97: Link AJ, Robison K, Church GM (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18(8);1259-313. PMID: 9298646

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Magnusson04a: Magnusson U, Salopek-Sondi B, Luck LA, Mowbray SL (2004). "X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity." J Biol Chem 279(10);8747-52. PMID: 14672931

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

Oxender80: Oxender DL, Anderson JJ, Daniels CJ, Landick R, Gunsalus RP, Zurawski G, Yanofsky C (1980). "Amino-terminal sequence and processing of the precursor of the leucine-specific binding protein, and evidence for conformational differences between the precursor and the mature form." Proc Natl Acad Sci U S A 77(4);2005-9. PMID: 6990419

Sack89: Sack JS, Trakhanov SD, Tsigannik IH, Quiocho FA (1989). "Structure of the L-leucine-binding protein refined at 2.4 A resolution and comparison with the Leu/Ile/Val-binding protein structure." J Mol Biol 206(1);193-207. PMID: 2649683

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.

UniProt11: UniProt Consortium (2011). "UniProt version 2011-06 released on 2011-06-30 00:00:00." Database.

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

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

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


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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 18.5 on Sun Dec 21, 2014, biocyc14.