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MetaCyc Enzyme: DNA-binding, ATP-dependent protease La

Gene: lon Accession Numbers: EG10542 (MetaCyc), b0439, ECK0433

Synonyms: capR, deg, dir, lopA, muc, Lon protease

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of DNA-binding, ATP-dependent protease La = [Lon]4

Summary:
Lon is an ATP-dependent protease responsible for degradation of misfolded proteins as well as a number of rapidly degraded regulatory proteins. Key regulatory proteins that are Lon substrates include the cell division regulator SulA [Schoemaker84, Higashitani97], the capsule synthesis regulator RcsA [TorresCabassa87] and possibly TER components involved in blocking septation sites during the SOS response [Dopazo87]. Lon is required for degradation of misfolded proteins and the prevention of aggregate formation [Chung81, Ryzhavskaia, Laskowska96]. In the absence of Lon function, aggregation triples [Rosen02]. At least some of this degradation of misfolded proteins depends on the chaperone DnaK [Sherman92].

Lon also degrades the lamba phage N and Xis proteins, with degradation of the latter promoting lysogeny over lysis [Maurizi87, Leffers98]. Other substrates included HU1 in the absence of its partner HU2, HemA and DAM methylase [Bonnefoy89, Wang99c, Calmann03].

Lon degrades the antitoxin protein in many toxin/antitoxin protein pairs, including both plasmid and chromosomal versions. Lon proteolysis of the antitoxin protein in plasmid-encoded pairs is required for plasmid maintenance, as the antitoxin has a shorter half life in lon+ cells than the toxin, thus requiring the continued presence of the plasmid for cell survival. Plasmid-encoded antitoxin substrates include CcdA from F plasmid, relBP307 and PasA [Van96a, Van94a, Gronlund99, Smith98c]. Lon proteolyzes chromosomal toxin/antoxin pairs as well, including RelB and YoeB [Christensen01, Christensen04]. This degradation of chromosomal pairs may regulate part of the starvation stress response, as the breakdown of RelB leaves RelE, which suppresses translation [Christensen01]. Starvation-induced transcription of chpA also depends on Lon [Christensen03].

Lon is an ATP-dependent protease with chymotrypsin-like specificity based on a Serine (679)-Lysine (722) dyad [Charette81, Waxman85, Botos04, Nishii05]. Lon has one proteolytic and four ATP-binding sites, two high affinity, the other two low affinity [Chin88, Menon87]. Detailed kinetic analysis shows that the two types of ATP sites use ATP at different rates as well [Vineyard06]. Lon's protease function depends on its ATPase activity; both require Mg2+, two ATP molecules are used per peptide bond hydrolyzed and loss of ATPase functions leads to concomitant loss of peptidase function [Menon87, Menon87a, Fischer94, Waxman82a]. ATPase activity continues in mutants that are unable to proteolyze [Pohl76]. Though its ATPase activity is required for protein degradation, Lon is capable of breaking down small peptides in the absence of ATP or ATPase function [Goldberg85, Rasulova98]. The isolated ATPase domain undergoes conformational change in response to ADP and ATP binding [Vasilyeva02].

Lon has an independent protein-binding domain in addition to its proteolytic domain. This domain binds unfolded proteins [Chin88]. Protein binding substantially stimulates peptide degradation and ATPase activity, the latter even in mutants incapable of peptidase function [Waxman86, Pohl76].

Lon binds DNA via its DNA-binding domain [Charette81, Chin88]. Addition of DNA, especially denatured DNA, stimulates substrate proteolysis in vitro, as well as stimulating ATPase activity even in the absence of substrate [Chung82, Charette84]. Lon may have specificity for promoter regions, explaining how it targets regulatory proteins [Fu97].

Lon can form a complex with inorganic polyphosphate, allowing subsequent degradation of ribosomal proteins, including S2, L9 and L13 [Kuroda01]. Lon's DNA-binding domain binds polyphosphate with greater affinity than DNA [Nomura04a]. Lon complexed with polyphosphate may be an octamer instead of a tetramer [Nishii05].

lon is one of a network of 93 genes believed to play a role in promoting the stress-induced mutagenesis (SIM) response of E. coli K-12 [Al12].

Locations: cytosol

Map Position: [458,112 -> 460,466]

Molecular Weight of Polypeptide: 87.438 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0001521 , CGSC:547 , DIP:DIP-35845N , EchoBASE:EB0537 , EcoGene:EG10542 , EcoliWiki:b0439 , EcoO157Cyc:LON-MONOMER , Mint:MINT-1224190 , ModBase:P0A9M0 , OU-Microarray:b0439 , PortEco:lon , PR:PRO_000023108 , Pride:P0A9M0 , Protein Model Portal:P0A9M0 , RefSeq:NP_414973 , RegulonDB:EG10542 , SMR:P0A9M0 , String:511145.b0439 , UniProt:P0A9M0

Relationship Links: InterPro:IN-FAMILY:IPR003111 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR003959 , InterPro:IN-FAMILY:IPR004815 , InterPro:IN-FAMILY:IPR008268 , InterPro:IN-FAMILY:IPR008269 , InterPro:IN-FAMILY:IPR014721 , InterPro:IN-FAMILY:IPR015947 , InterPro:IN-FAMILY:IPR020568 , InterPro:IN-FAMILY:IPR027065 , InterPro:IN-FAMILY:IPR027417 , InterPro:IN-FAMILY:IPR027543 , Panther:IN-FAMILY:PTHR10046 , PDB:Structure:1QZM , PDB:Structure:1RR9 , PDB:Structure:1RRE , PDB:Structure:2ANE , PDB:Structure:3LJC , Pfam:IN-FAMILY:PF00004 , Pfam:IN-FAMILY:PF02190 , Pfam:IN-FAMILY:PF05362 , Prosite:IN-FAMILY:PS01046 , Smart:IN-FAMILY:SM00382 , Smart:IN-FAMILY:SM00464

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis Inferred from experiment [Rasulova98, Charette81, Gaudet10, GOA06, GOA01]
GO:0006508 - proteolysis Inferred from experiment Inferred by computational analysis [UniProtGOA11, GOA01, Charette81]
GO:0009408 - response to heat Inferred from experiment [Chuang93]
GO:0006515 - misfolded or incompletely synthesized protein catabolic process Inferred by computational analysis [GOA06, Gaudet10]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
GO:0030163 - protein catabolic process Inferred by computational analysis [GOA01]
GO:0033554 - cellular response to stress Inferred by computational analysis [GOA06]
Molecular Function: GO:0003677 - DNA binding Inferred from experiment [Fu97]
GO:0004176 - ATP-dependent peptidase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Gaudet10, Rasulova98, Charette81]
GO:0004252 - serine-type endopeptidase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, Rotanova04]
GO:0005515 - protein binding Inferred from experiment [Redelberger13]
GO:0008233 - peptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Rasulova98]
GO:0016887 - ATPase activity Inferred from experiment [Charette81]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA06, GOA01]
GO:0008236 - serine-type peptidase activity Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0043565 - sequence-specific DNA binding Inferred by computational analysis [GOA06, GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, GOA06, Gaudet10, Fu97]
GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]

MultiFun Terms: cell processes cell division
extrachromosomal plasmid related
extrachromosomal prophage genes and phage related functions
information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides
regulation type of regulation posttranscriptional proteases, cleavage of compounds

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: serine protease (DNA-binding, ATP-dependent protease La)

EC Number: 3.4.21.53

a protein + H2O <=> a peptide + a peptide

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is physiologically favored in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
This is a serine protease activity with chymotrypsin-like specificity [Charette81, Waxman85, Botos04]. Peptide hydrolysis is ATP independent in vitro, but protein degradation is ATP dependent, requiring 2 ATP per peptide bond hydrolyzed [Menon87a].

pH(opt): 7.8 [BRENDA14, Goldberg92], 9 [BRENDA14, Waxman85]


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[Fu97, UniProt11a]
UniProt: Removed.
Chain 2 -> 784
[UniProt10]
UniProt: Lon protease;
Conserved-Region 10 -> 201
[UniProt10]
UniProt: Lon;
Protein-Segment 211 -> 219
[UniProt09]
UniProt: Arg/Lys-rich (basic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 240 -> 252
[UniProt09]
UniProt: Asp/Glu-rich (acidic); Sequence Annotation Type: compositionally biased region;
Protein-Segment 255 -> 270
[UniProt09]
UniProt: Arg/Lys-rich (basic); Sequence Annotation Type: compositionally biased region;
Sequence-Conflict 264 -> 317
[Chin88, UniProt10]
Alternate sequence: RKRQKRKRTGVAEAENDVSDVGRSDRSAWLYRLDGTGAVECAYEGQKRPASGA; UniProt: (in Ref. 5);
Sequence-Conflict 273
[Fischer93a, UniProt10]
Alternate sequence: R; UniProt: (in Ref. 4; AAA16837);
Sequence-Conflict 307
[Fischer93a, UniProt10]
Alternate sequence: T; UniProt: (in Ref. 4; AAA16837);
Nucleotide-Phosphate-Binding-Region 356 -> 363
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Mutagenesis-Variant 362
[Fischer94, UniProt11a]
Alternate sequence: A; UniProt: Loss of proteolytic activity and ATP-binding.
Sequence-Conflict 539 -> 563
[Chin88, UniProt10]
Alternate sequence: RACVVWSVKSPNCVAKRLSSYCSIT; UniProt: (in Ref. 5; AAA24078);
Mutagenesis-Variant 665
[Starkova98, UniProt11a]
Alternate sequence: Y; UniProt: Loss of proteolytic activity.
Mutagenesis-Variant 667
[Starkova98, UniProt11a]
Alternate sequence: Y; UniProt: Loss of proteolytic activity.
Mutagenesis-Variant 676
[Starkova98, UniProt11a]
Alternate sequence: N; UniProt: Loss of proteolytic activity.
Mutagenesis-Variant 679
[Fischer93a, UniProt11a]
Alternate sequence: A; UniProt: Loss of proteolytic activity.
Active-Site 679
[UniProt10]
Active-Site 722
[Botos04, UniProt11a]
.
Mutagenesis-Variant 743
[Starkova98, UniProt11a]
Alternate sequence: N; UniProt: No effect.
Sequence-Conflict 772
[Fischer93a, UniProt10]
Alternate sequence: R; UniProt: (in Ref. 4; AAA16837);
Sequence-Conflict 779 -> 784
[Amerik88, UniProt10]
Alternate sequence: HHSLRRRCSTASTYYWAKS; UniProt: (in Ref. 2);

History:
10/20/97 Gene b0439 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10542; confirmed by SwissProt match.


References

Al12: Al Mamun AA, Lombardo MJ, Shee C, Lisewski AM, Gonzalez C, Lin D, Nehring RB, Saint-Ruf C, Gibson JL, Frisch RL, Lichtarge O, Hastings PJ, Rosenberg SM (2012). "Identity and function of a large gene network underlying mutagenic repair of DNA breaks." Science 338(6112);1344-8. PMID: 23224554

Amerik88: Amerik AIu, Chistiakov LG, Ostroumova NI, Gurevich AI, Antonov VK (1988). "[Cloning, expression and structure of the functionally active shortened lon gene in Escherichia coli]." Bioorg Khim 14(3);408-11. PMID: 3289547

Bonnefoy89: Bonnefoy E, Almeida A, Rouviere-Yaniv J (1989). "Lon-dependent regulation of the DNA binding protein HU in Escherichia coli." Proc Natl Acad Sci U S A 86(20);7691-5. PMID: 2682620

Botos04: Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A (2004). "The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site." J Biol Chem 279(9);8140-8. PMID: 14665623

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

Calmann03: Calmann MA, Marinus MG (2003). "Regulated expression of the Escherichia coli dam gene." J Bacteriol 185(16);5012-4. PMID: 12897023

Charette81: Charette MF, Henderson GW, Markovitz A (1981). "ATP hydrolysis-dependent protease activity of the lon (capR) protein of Escherichia coli K-12." Proc Natl Acad Sci U S A 78(8);4728-32. PMID: 6458036

Charette84: Charette MF, Henderson GW, Doane LL, Markovitz A (1984). "DNA-stimulated ATPase activity on the lon (CapR) protein." J Bacteriol 158(1);195-201. PMID: 6325386

Chin88: Chin DT, Goff SA, Webster T, Smith T, Goldberg AL (1988). "Sequence of the lon gene in Escherichia coli. A heat-shock gene which encodes the ATP-dependent protease La." J Biol Chem 263(24);11718-28. PMID: 3042779

Christensen01: Christensen SK, Mikkelsen M, Pedersen K, Gerdes K (2001). "RelE, a global inhibitor of translation, is activated during nutritional stress." Proc Natl Acad Sci U S A 98(25);14328-33. PMID: 11717402

Christensen03: Christensen SK, Pedersen K, Hansen FG, Gerdes K (2003). "Toxin-antitoxin loci as stress-response-elements: ChpAK/MazF and ChpBK cleave translated RNAs and are counteracted by tmRNA." J Mol Biol 332(4);809-19. PMID: 12972253

Christensen04: Christensen SK, Maenhaut-Michel G, Mine N, Gottesman S, Gerdes K, Van Melderen L (2004). "Overproduction of the Lon protease triggers inhibition of translation in Escherichia coli: involvement of the yefM-yoeB toxin-antitoxin system." Mol Microbiol 51(6);1705-17. PMID: 15009896

Chuang93: Chuang SE, Blattner FR (1993). "Characterization of twenty-six new heat shock genes of Escherichia coli." J Bacteriol 175(16);5242-52. PMID: 8349564

Chung81: Chung CH, Goldberg AL (1981). "The product of the lon (capR) gene in Escherichia coli is the ATP-dependent protease, protease La." Proc Natl Acad Sci U S A 78(8);4931-5. PMID: 6458037

Chung82: Chung CH, Goldberg AL (1982). "DNA stimulates ATP-dependent proteolysis and protein-dependent ATPase activity of protease La from Escherichia coli." Proc Natl Acad Sci U S A 79(3);795-9. PMID: 6461007

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

Dopazo87: Dopazo A, Tormo A, Aldea M, Vicente M (1987). "Structural inhibition and reactivation of Escherichia coli septation by elements of the SOS and TER pathways." J Bacteriol 169(4);1772-6. PMID: 3031022

Fischer93a: Fischer H, Glockshuber R (1993). "ATP hydrolysis is not stoichiometrically linked with proteolysis in the ATP-dependent protease La from Escherichia coli." J Biol Chem 268(30);22502-7. PMID: 8226758

Fischer94: Fischer H, Glockshuber R (1994). "A point mutation within the ATP-binding site inactivates both catalytic functions of the ATP-dependent protease La (Lon) from Escherichia coli." FEBS Lett 356(1);101-3. PMID: 7988699

Fu97: Fu GK, Smith MJ, Markovitz DM (1997). "Bacterial protease Lon is a site-specific DNA-binding protein." J Biol Chem 272(1);534-8. PMID: 8995294

Gaudet10: Gaudet P, Livstone M, Thomas P (2010). "Annotation inferences using phylogenetic trees." PMID: 19578431

GOA01: 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."

Goldberg85: Goldberg AL, Waxman L (1985). "The role of ATP hydrolysis in the breakdown of proteins and peptides by protease La from Escherichia coli." J Biol Chem 260(22);12029-34. PMID: 2931432

Goldberg92: Goldberg AL (1992). "The mechanism and functions of ATP-dependent proteases in bacterial and animal cells." Eur J Biochem 203(1-2);9-23. PMID: 1730246

Gronlund99: Gronlund H, Gerdes K (1999). "Toxin-antitoxin systems homologous with relBE of Escherichia coli plasmid P307 are ubiquitous in prokaryotes." J Mol Biol 285(4);1401-15. PMID: 9917385

Higashitani97: Higashitani A, Ishii Y, Kato Y, Koriuchi K (1997). "Functional dissection of a cell-division inhibitor, SulA, of Escherichia coli and its negative regulation by Lon." Mol Gen Genet 254(4);351-7. PMID: 9180687

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Kuroda01: Kuroda A, Nomura K, Ohtomo R, Kato J, Ikeda T, Takiguchi N, Ohtake H, Kornberg A (2001). "Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli." Science 293(5530);705-8. PMID: 11474114

Laskowska96: Laskowska E, Kuczynska-Wisnik D, Skorko-Glonek J, Taylor A (1996). "Degradation by proteases Lon, Clp and HtrA, of Escherichia coli proteins aggregated in vivo by heat shock; HtrA protease action in vivo and in vitro." Mol Microbiol 22(3);555-71. PMID: 8939438

Leffers98: Leffers GG, Gottesman S (1998). "Lambda Xis degradation in vivo by Lon and FtsH." J Bacteriol 180(6);1573-7. PMID: 9515930

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

Maurizi87: Maurizi MR (1987). "Degradation in vitro of bacteriophage lambda N protein by Lon protease from Escherichia coli." J Biol Chem 262(6);2696-703. PMID: 2950089

Menon87: Menon AS, Goldberg AL (1987). "Binding of nucleotides to the ATP-dependent protease La from Escherichia coli." J Biol Chem 262(31);14921-8. PMID: 3312196

Menon87a: Menon AS, Waxman L, Goldberg AL (1987). "The energy utilized in protein breakdown by the ATP-dependent protease (La) from Escherichia coli." J Biol Chem 262(2);722-6. PMID: 2948950

Nishii05: Nishii W, Suzuki T, Nakada M, Kim YT, Muramatsu T, Takahashi K (2005). "Cleavage mechanism of ATP-dependent Lon protease toward ribosomal S2 protein." FEBS Lett 579(30);6846-50. PMID: 16337203

Nomura04a: Nomura K, Kato J, Takiguchi N, Ohtake H, Kuroda A (2004). "Effects of inorganic polyphosphate on the proteolytic and DNA-binding activities of Lon in Escherichia coli." J Biol Chem 279(33);34406-10. PMID: 15187082

Pohl76: Pohl A, Bugajer-Gleitman HE, Lachmann D, Moser K (1976). "[Glutathione reductase deficiency with membrane defect in hereditary hemolytic anemia]." Acta Haematol 56(1);47-57. PMID: 822675

Rasulova98: Rasulova FS, Dergousova NI, Starkova NN, Melnikov EE, Rumsh LD, Ginodman LM, Rotanova TV (1998). "The isolated proteolytic domain of Escherichia coli ATP-dependent protease Lon exhibits the peptidase activity." FEBS Lett 432(3);179-81. PMID: 9720920

Redelberger13: Redelberger D, Genest O, Arabet D, Mejean V, Ilbert M, Iobbi-Nivol C (2013). "Quality control of a molybdoenzyme by the Lon protease." FEBS Lett 587(24);3935-42. PMID: 24211448

Rosen02: Rosen R, Biran D, Gur E, Becher D, Hecker M, Ron EZ (2002). "Protein aggregation in Escherichia coli: role of proteases." FEMS Microbiol Lett 207(1);9-12. PMID: 11886743

Rotanova04: Rotanova TV, Melnikov EE, Khalatova AG, Makhovskaya OV, Botos I, Wlodawer A, Gustchina A (2004). "Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains." Eur J Biochem 271(23-24);4865-71. PMID: 15606774

Ryzhavskaia: Ryzhavskaia AS, Kaidalova NV, Anukhin IuM, Kliachko EV, Livshits VA "[Stability of normal, abnormal and recombinant proteins in Escherichia coli strains deficient for intracellular proteinase La--the product of the lon gene]." Mol Biol (Mosk) 22(1);201-8. PMID: 3287135

Schoemaker84: Schoemaker JM, Gayda RC, Markovitz A (1984). "Regulation of cell division in Escherichia coli: SOS induction and cellular location of the sulA protein, a key to lon-associated filamentation and death." J Bacteriol 158(2);551-61. PMID: 6327610

Sherman92: Sherman MYu , Goldberg AL (1992). "Involvement of the chaperonin dnaK in the rapid degradation of a mutant protein in Escherichia coli." EMBO J 11(1);71-7. PMID: 1740117

Smith98c: Smith AS, Rawlings DE (1998). "Efficiency of the pTF-FC2 pas poison-antidote stability system in Escherichia coli is affected by the host strain, and antidote degradation requires the lon protease." J Bacteriol 180(20);5458-62. PMID: 9765581

Starkova98: Starkova NN, Koroleva EP, Rumsh LD, Ginodman LM, Rotanova TV (1998). "Mutations in the proteolytic domain of Escherichia coli protease Lon impair the ATPase activity of the enzyme." FEBS Lett 422(2);218-20. PMID: 9490010

TorresCabassa87: Torres-Cabassa AS, Gottesman S (1987). "Capsule synthesis in Escherichia coli K-12 is regulated by proteolysis." J Bacteriol 169(3);981-9. PMID: 3029041

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.

UniProt11a: 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."

Van94a: Van Melderen L, Bernard P, Couturier M (1994). "Lon-dependent proteolysis of CcdA is the key control for activation of CcdB in plasmid-free segregant bacteria." Mol Microbiol 11(6);1151-7. PMID: 8022284

Van96a: Van Melderen L, Thi MH, Lecchi P, Gottesman S, Couturier M, Maurizi MR (1996). "ATP-dependent degradation of CcdA by Lon protease. Effects of secondary structure and heterologous subunit interactions." J Biol Chem 271(44);27730-8. PMID: 8910366

Vasilyeva02: Vasilyeva OV, Kolygo KB, Leonova YF, Potapenko NA, Ovchinnikova TV (2002). "Domain structure and ATP-induced conformational changes in Escherichia coli protease Lon revealed by limited proteolysis and autolysis." FEBS Lett 526(1-3);66-70. PMID: 12208506

Vineyard06: Vineyard D, Zhang X, Lee I (2006). "Transient kinetic experiments demonstrate the existence of a unique catalytic enzyme form in the peptide-stimulated ATPase mechanism of Escherichia coli Lon protease." Biochemistry 45(38);11432-43. PMID: 16981703

Wang99c: Wang L, Elliott M, Elliott T (1999). "Conditional stability of the HemA protein (glutamyl-tRNA reductase) regulates heme biosynthesis in Salmonella typhimurium." J Bacteriol 181(4);1211-9. PMID: 9973348

Waxman82a: Waxman L, Goldberg AL (1982). "Protease La from Escherichia coli hydrolyzes ATP and proteins in a linked fashion." Proc Natl Acad Sci U S A 79(16);4883-7. PMID: 6214787

Waxman85: Waxman L, Goldberg AL (1985). "Protease La, the lon gene product, cleaves specific fluorogenic peptides in an ATP-dependent reaction." J Biol Chem 260(22);12022-8. PMID: 3900067

Waxman86: Waxman L, Goldberg AL (1986). "Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La)." Science 232(4749);500-3. PMID: 2938257


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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