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Escherichia coli K-12 substr. MG1655 Protein: ClpA ATP-dependent protease specificity component and chaperone



Gene: clpA Accession Numbers: EG10156 (EcoCyc), b0882, ECK0873

Synonyms: cipA, lopD, ATP-binding component of serine protease

Regulation Summary Diagram: ?

Component of:
ClpAXP (summary available)
ClpAP (extended summary available)

Subunit composition of ClpA ATP-dependent protease specificity component and chaperone = [ClpA]6

Summary:
ClpA is an ATP-dependent molecular chaperone that serves as a substrate-specifying adapter for the ClpP serine protease in the ClpAP and ClpAXP protease complexes.

In its capacity as a chaperone, ClpA activates the RepA replication initiator protein of plasmid F1 in an ATP-dependent manner, converting it from a dimer to a monomer [Wickner94]. This activity requires interaction between ClpA and the amino-terminus of RepA [Hoskins00]. Should the RepA amino-terminus be blocked, ClpA can still interact with it as long as there is an accessible amino acid tract at the RepA carboxy-terminus [Hoskins06].

ClpA lacking its own amino-terminal domain is still able to function as both chaperone and protease adaptor, though it is less effective in both roles than the wild-type protein [Lo01].

Each ClpA monomer has two domains, leading to a double-stacked ring structure in the complete ClpA hexamer [Beuron98]. The putative substrate-recognition domain of ClpA is stable and folds independently, unlike the matching domains in ClpB and ClpX [Smith99]. Each ClpA monomer has two AAA+ modules (consensus ATP-binding sites), the first of which interacts with the amino-terminal domain of the protein [Gottesman90, Guo02a]. A lysine mutation in either ATP-binding site prevents the ATP-dependent formation of the ClpA hexamer, as well as disrupting ATPase activity and removing the ability to activate ClpP. Mutants in the second ATP-binding site were still able to stimulate degradation of some shorter peptide substrates requiring nucleotide binding, but not hydrolysis [Singh94, Seol95a].

The ClpA hexamer forms in an ATP-dependent manner [Kessel95]. Successful formation of the hexamer and subsequent interaction with ClpP requires the carboxy-terminus of ClpA. In its ATP-bound state, ClpA is protease resistant [Singh01].

ClpA is required for the ATP-dependent degradation of certain substrates by ClpP, including some abnormal proteins and the in vitro test substrate casein [Katayama88, Hinnerwisch05]. ClpA binds to the SsrA degradation peptide tag, with one tag binding per ClpA hexamer. This interaction does not depend on either ATP-binding domain in ClpA [Piszczek05]. The amino-terminal domain of ClpA is required for binding nonspecific protein substrates that have not been tagged with SsrA [Xia04a].

NEM inhibits ClpA function by introducing a bulky alkyl group but not by directly binding to a catalytic residue [Seol97].

ClpA is required for maximal growth in SDS, normal adaptation to and extended viability in stationary phase and for activity of bacteriophage Mu [Rajagopal02, Weichart03, Shapiro93].

The clpA gene contains a sequence for an internal translational initiation and therefore encode two polypeptides with different sizes (ClpA65 and ClpA84) [Seol94]. The 65 kDa form prevents degradation of ClpA by ClpAP [Seol95b].

ClpS binds to the ClpA amino-terminus and affects the specificity of protein degradation by the ClpAP chaperone-protease complex, possibly by interfering with interactions between substrate and ClpA [Dougan02]. ClpS stimulates ClpAP recognition and degradation of aggregated protein substrates while it inhibits degradation of non-aggregated substrates including ClpA [Dougan02].

A crystal structure of the ClpA N terminus shows a zinc binding site [Guo02b]. Crystal structures of ClpS bound to the N-terminal region of ClpA are presented at 2.3 Å [Guo02b], 2.5 Å [Zeth02], and 3.3 Å [Guo02b] resolution.

clpA shows differential codon adaptation, resulting in differential translation efficiency signatures, in aerotolerant compared to obligate anaerobic microbes. It was therefore predicted to play a role in the oxidative stress response. A clpA deletion mutant was shown to be more sensitive than wild-type specifically to hydrogen peroxide exposure, but not other stresses [Krisko14].

Locations: cytosol

Map Position: [922,487 -> 924,763] (19.88 centisomes)
Length: 2277 bp / 758 aa

Molecular Weight of Polypeptide: 84.207 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003001 , CGSC:31293 , DIP:DIP-35409N , EchoBASE:EB0154 , EcoGene:EG10156 , EcoliWiki:b0882 , ModBase:P0ABH9 , OU-Microarray:b0882 , PortEco:clpA , PR:PRO_000022296 , Pride:P0ABH9 , Protein Model Portal:P0ABH9 , RefSeq:NP_415403 , RegulonDB:EG10156 , SMR:P0ABH9 , String:511145.b0882 , UniProt:P0ABH9

Relationship Links: InterPro:IN-FAMILY:IPR001270 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR003959 , InterPro:IN-FAMILY:IPR004176 , InterPro:IN-FAMILY:IPR013093 , InterPro:IN-FAMILY:IPR013461 , InterPro:IN-FAMILY:IPR018368 , InterPro:IN-FAMILY:IPR019489 , InterPro:IN-FAMILY:IPR023150 , InterPro:IN-FAMILY:IPR027417 , InterPro:IN-FAMILY:IPR028299 , Panther:IN-FAMILY:PTHR11638:SF14 , PDB:Structure:1K6K , PDB:Structure:1KSF , PDB:Structure:1LZW , PDB:Structure:1MBU , PDB:Structure:1MBV , PDB:Structure:1MBX , PDB:Structure:1MG9 , PDB:Structure:1R6B , PDB:Structure:1R6C , PDB:Structure:1R6O , PDB:Structure:1R6Q , Pfam:IN-FAMILY:PF00004 , Pfam:IN-FAMILY:PF02861 , Pfam:IN-FAMILY:PF07724 , Pfam:IN-FAMILY:PF10431 , Prints:IN-FAMILY:PR00300 , Prosite:IN-FAMILY:PS00870 , Prosite:IN-FAMILY:PS00871 , Smart:IN-FAMILY:SM00382 , Smart:IN-FAMILY:SM01086

In Paralogous Gene Group: 221 (2 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred from experiment [Katayama88]
GO:0006979 - response to oxidative stress Inferred from experiment [Krisko14]
GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01]
GO:0019538 - protein metabolic process Inferred by computational analysis [GOA01]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Hauser14, Rajagopala14, Schmidt09, Butland05, Xia04a, Zeth02, Guo02b]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11]
GO:0004176 - ATP-dependent peptidase activity Inferred by computational analysis [GOA01]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11, GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]

MultiFun Terms: information transfer protein related chaperoning, repair (refolding)
information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides

Essentiality data for clpA 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]

Credits:
Revised 25-May-2011 by Brito D


Subunit of: ClpAXP

Synonyms: ATP-dependent endopeptidase Clp, ATP-dependent protease Clp

Subunit composition of ClpAXP = [(ClpP)14][(ClpA)6][(ClpX)6]
         ClpP serine protease = (ClpP)14 (extended summary available)
         ClpA ATP-dependent protease specificity component and chaperone = (ClpA)6
         ClpX ATP-dependent protease specificity component and chaperone = (ClpX)6 (extended summary available)

Summary:
Hybrid complexes can form in vitro, consisting of a ClpP tetradecamer capped at one end with ClpA and at the other with ClpX. These complexes are translocation competent. Stoichiometry in vivo suggests heterocomplexes may form there, as well [Ortega04].


Enzymatic reaction of: ATP-dependent Clp protease (ClpAXP)

Synonyms: ATP-binding Clp protease, ATP-dependent Clp endopeptidase

EC Number: 3.4.21.92

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.


Subunit of: ClpAP

Subunit composition of ClpAP = [(ClpP)14][(ClpA)6]2
         ClpP serine protease = (ClpP)14 (extended summary available)
         ClpA ATP-dependent protease specificity component and chaperone = (ClpA)6

Summary:
ClpAP is a serine protease complex responsible for the ATP-dependent degradation of a number of proteins [Katayama88]. Substrates for ClpAP include the plasmid P1 replication intiator RepA, HemA and a number of carbon starvation proteins [Wickner94, Wang99c, Damerau93]. ClpAP is also one of the proteases responsible for degradation of proteins tagged with the SsrA degradation marker, including tagged lambda repressor and tagged GFP (the latter substrate indicating that ClpAP can unfold stable, native protein in an ATP-dependent manner) [Gottesman98, WeberBan99]. ClpAP degrades a number of substrates that are not degraded by ClpXP [Gottesman93]. ClpAP is also responsible for rapid degradation of N-end rule substrates, which are marked for degradation by the identity of their amino-terminal residue (arginine, lysine, leucine, phenylalanine, tyrosine and tryptophan all mark a protein for N-end rule degradation) [Tobias91].

ClpAP consists of a ClpP tetradecamer capped at one or both ends by ClpA hexamers [Kessel95, Ishikawa]. The formation of this complex requires ATP binding and hydrolysis [Thompson94, Seol95, Maurizi98]. ATP is also required for degradation of larger polypeptide substrates by ClpAP [Thompson94]. ClpAP remains together as a complex through repeated rounds of degradation [Singh99]. ClpAP substrates interact with an allosteric site on ClpA prior to proteolysis by ClpP [Thompson94a].

A putative internal translation site variant of ClpA inhibits the interaction of full-length ClpA with ClpP, preventing formation of ClpAP [Seol94].

ClpS binds to the amino-terminal domain of ClpA, inhibiting degradation of SsrA-tagged proteins and of ClpA but accelerating disaggregation and degradation of heat-aggregated proteins in vitro [Dougan02, Zeth02].

ClpA levels increase during late exponential and early stationary phase, resulting in an increase in ClpAP activity [Katayama90].

ClpAP is required to maintain translation of the DNA protection protein Dps during starvation [Stephani03].


Enzymatic reaction of: ClpAP

EC Number: 3.4.21.92

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.


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 20, 22, 63
[Guo02b]
The amino-terminus of ClpA contains a Zinc binding site.
Protein-Segment 169 -> 417
[UniProt10a]
UniProt: I; Sequence Annotation Type: region of interest;
Nucleotide-Phosphate-Binding-Region 214 -> 221
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 367
[Gottesman90, UniProt10]
Alternate sequence: A → G; UniProt: (in Ref. 1; AAA23583);
Sequence-Conflict 411
[Gottesman90, UniProt10]
Alternate sequence: L → V; UniProt: (in Ref. 1; AAA23583);
Protein-Segment 421 -> 609
[UniProt10a]
UniProt: II; Sequence Annotation Type: region of interest;
Nucleotide-Phosphate-Binding-Region 495 -> 502
[UniProt10a]
UniProt: ATP; Non-Experimental Qualifier: potential;
Sequence-Conflict 533
[Gottesman90, UniProt10]
Alternate sequence: L → V; UniProt: (in Ref. 1; AAA23583);


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b0882 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10156; confirmed by SwissProt match.


References

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Beuron98: Beuron F, Maurizi MR, Belnap DM, Kocsis E, Booy FP, Kessel M, Steven AC (1998). "At sixes and sevens: characterization of the symmetry mismatch of the ClpAP chaperone-assisted protease." J Struct Biol 123(3);248-59. PMID: 9878579

Butland05: Butland G, Peregrin-Alvarez JM, Li J, Yang W, Yang X, Canadien V, Starostine A, Richards D, Beattie B, Krogan N, Davey M, Parkinson J, Greenblatt J, Emili A (2005). "Interaction network containing conserved and essential protein complexes in Escherichia coli." Nature 433(7025);531-7. PMID: 15690043

Damerau93: Damerau K, St John AC (1993). "Role of Clp protease subunits in degradation of carbon starvation proteins in Escherichia coli." J Bacteriol 175(1);53-63. PMID: 8416909

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

Dougan02: Dougan DA, Reid BG, Horwich AL, Bukau B (2002). "ClpS, a substrate modulator of the ClpAP machine." Mol Cell 2002;9(3);673-83. PMID: 11931773

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."

Gottesman90: Gottesman S, Clark WP, Maurizi MR (1990). "The ATP-dependent Clp protease of Escherichia coli. Sequence of clpA and identification of a Clp-specific substrate." J Biol Chem 1990;265(14);7886-93. PMID: 2186030

Gottesman93: Gottesman S, Clark WP, de Crecy-Lagard V, Maurizi MR (1993). "ClpX, an alternative subunit for the ATP-dependent Clp protease of Escherichia coli. Sequence and in vivo activities." J Biol Chem 1993;268(30);22618-26. PMID: 8226770

Gottesman98: Gottesman S, Roche E, Zhou Y, Sauer RT (1998). "The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system." Genes Dev 12(9);1338-47. PMID: 9573050

Guo02a: Guo F, Maurizi MR, Esser L, Xia D (2002). "Crystal structure of ClpA, an Hsp100 chaperone and regulator of ClpAP protease." J Biol Chem 277(48);46743-52. PMID: 12205096

Guo02b: Guo F, Esser L, Singh SK, Maurizi MR, Xia D (2002). "Crystal structure of the heterodimeric complex of the adaptor, ClpS, with the N-domain of the AAA+ chaperone, ClpA." J Biol Chem 277(48);46753-62. PMID: 12235156

Hauser14: Hauser R, Ceol A, Rajagopala SV, Mosca R, Siszler G, Wermke N, Sikorski P, Schwarz F, Schick M, Wuchty S, Aloy P, Uetz P (2014). "A Second-generation Protein-Protein Interaction Network of Helicobacter pylori." Mol Cell Proteomics 13(5);1318-29. PMID: 24627523

Hinnerwisch05: Hinnerwisch J, Fenton WA, Furtak KJ, Farr GW, Horwich AL (2005). "Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation." Cell 121(7);1029-41. PMID: 15989953

Hoskins00: Hoskins JR, Kim SY, Wickner S (2000). "Substrate recognition by the ClpA chaperone component of ClpAP protease." J Biol Chem 275(45);35361-7. PMID: 10952988

Hoskins06: Hoskins JR, Wickner S (2006). "Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP." Proc Natl Acad Sci U S A 103(4);909-14. PMID: 16410355

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

Ishikawa: Ishikawa T, Maurizi MR, Steven AC "The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease." J Struct Biol 146(1-2);180-8. PMID: 15037249

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

Katayama88: Katayama Y, Gottesman S, Pumphrey J, Rudikoff S, Clark WP, Maurizi MR (1988). "The two-component, ATP-dependent Clp protease of Escherichia coli. Purification, cloning, and mutational analysis of the ATP-binding component." J Biol Chem 263(29);15226-36. PMID: 3049606

Katayama90: Katayama Y, Kasahara A, Kuraishi H, Amano F (1990). "Regulation of activity of an ATP-dependent protease, Clp, by the amount of a subunit, ClpA, in the growth of Escherichia coli cells." J Biochem (Tokyo) 108(1);37-41. PMID: 2121722

Kessel95: Kessel M, Maurizi MR, Kim B, Kocsis E, Trus BL, Singh SK, Steven AC (1995). "Homology in structural organization between E. coli ClpAP protease and the eukaryotic 26 S proteasome." J Mol Biol 250(5);587-94. PMID: 7623377

Krisko14: Krisko A, Copi T, Gabaldon T, Lehner B, Supek F (2014). "Inferring gene function from evolutionary change in signatures of translation efficiency." Genome Biol 15(3);R44. PMID: 24580753

Lo01: Lo JH, Baker TA, Sauer RT (2001). "Characterization of the N-terminal repeat domain of Escherichia coli ClpA-A class I Clp/HSP100 ATPase." Protein Sci 10(3);551-9. PMID: 11344323

Maurizi98: Maurizi MR, Singh SK, Thompson MW, Kessel M, Ginsburg A (1998). "Molecular properties of ClpAP protease of Escherichia coli: ATP-dependent association of ClpA and clpP." Biochemistry 37(21);7778-86. PMID: 9601038

Ortega04: Ortega J, Lee HS, Maurizi MR, Steven AC (2004). "ClpA and ClpX ATPases bind simultaneously to opposite ends of ClpP peptidase to form active hybrid complexes." J Struct Biol 146(1-2);217-26. PMID: 15037252

Piszczek05: Piszczek G, Rozycki J, Singh SK, Ginsburg A, Maurizi MR (2005). "The molecular chaperone, ClpA has a single high affinity peptide binding site per hexamer." J Biol Chem 280(13):12221-30. PMID: 15657062

Rajagopal02: Rajagopal S, Sudarsan N, Nickerson KW (2002). "Sodium dodecyl sulfate hypersensitivity of clpP and clpB mutants of Escherichia coli." Appl Environ Microbiol 68(8);4117-21. PMID: 12147516

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Schmidt09: Schmidt R, Zahn R, Bukau B, Mogk A (2009). "ClpS is the recognition component for Escherichia coli substrates of the N-end rule degradation pathway." Mol Microbiol 72(2);506-17. PMID: 19317833

Seol94: Seol JH, Yoo SJ, Kim KI, Kang MS, Ha DB, Chung CH (1994). "The 65-kDa protein derived from the internal translational initiation site of the clpA gene inhibits the ATP-dependent protease Ti in Escherichia coli." J Biol Chem 269(47);29468-73. PMID: 7961929

Seol95: Seol JH, Woo KM, Kang MS, Ha DB, Chung CH (1995). "Requirement of ATP hydrolysis for assembly of ClpA/ClpP complex, the ATP-dependent protease Ti in Escherichia coli." Biochem Biophys Res Commun 217(1);41-51. PMID: 8526938

Seol95a: Seol JH, Baek SH, Kang MS, Ha DB, Chung CH (1995). "Distinctive roles of the two ATP-binding sites in ClpA, the ATPase component of protease Ti in Escherichia coli." J Biol Chem 270(14);8087-92. PMID: 7713911

Seol95b: Seol JH, Yoo SJ, Kang MS, Ha DB, Chung CH (1995). "The 65-kDa protein derived from the internal translational start site of the clpA gene blocks autodegradation of ClpA by the ATP-dependent protease Ti in Escherichia coli." FEBS Lett 377(1);41-3. PMID: 8543014

Seol97: Seol JH, Kwon JA, Yoo SJ, Kim HS, Kang MS, Chung CH (1997). "Site-directed mutagenesis of the Cys residues in ClpA, the ATPase component of protease Ti (ClpAP) in Escherichia coli." Biol Chem 378(10);1205-9. PMID: 9372193

Shapiro93: Shapiro JA (1993). "A role for the Clp protease in activating Mu-mediated DNA rearrangements." J Bacteriol 175(9);2625-31. PMID: 8386721

Singh01: Singh SK, Rozycki J, Ortega J, Ishikawa T, Lo J, Steven AC, Maurizi MR (2001). "Functional domains of the ClpA and ClpX molecular chaperones identified by limited proteolysis and deletion analysis." J Biol Chem 276(31);29420-9. PMID: 11346657

Singh94: Singh SK, Maurizi MR (1994). "Mutational analysis demonstrates different functional roles for the two ATP-binding sites in ClpAP protease from Escherichia coli." J Biol Chem 269(47);29537-45. PMID: 7961938

Singh99: Singh SK, Guo F, Maurizi MR (1999). "ClpA and ClpP remain associated during multiple rounds of ATP-dependent protein degradation by ClpAP protease." Biochemistry 38(45);14906-15. PMID: 10555973

Smith99: Smith CK, Baker TA, Sauer RT (1999). "Lon and Clp family proteases and chaperones share homologous substrate-recognition domains." Proc Natl Acad Sci U S A 96(12);6678-82. PMID: 10359771

Stephani03: Stephani K, Weichart D, Hengge R (2003). "Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli." Mol Microbiol 49(6);1605-14. PMID: 12950924

Thompson94: Thompson MW, Singh SK, Maurizi MR (1994). "Processive degradation of proteins by the ATP-dependent Clp protease from Escherichia coli. Requirement for the multiple array of active sites in ClpP but not ATP hydrolysis." J Biol Chem 269(27);18209-15. PMID: 8027082

Thompson94a: Thompson MW, Maurizi MR (1994). "Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates." J Biol Chem 269(27);18201-8. PMID: 8027081

Tobias91: Tobias JW, Shrader TE, Rocap G, Varshavsky A (1991). "The N-end rule in bacteria." Science 254(5036);1374-7. PMID: 1962196

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.

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

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

WeberBan99: Weber-Ban EU, Reid BG, Miranker AD, Horwich AL (1999). "Global unfolding of a substrate protein by the Hsp100 chaperone ClpA." Nature 401(6748);90-3. PMID: 10485712

Weichart03: Weichart D, Querfurth N, Dreger M, Hengge-Aronis R (2003). "Global role for ClpP-containing proteases in stationary-phase adaptation of Escherichia coli." J Bacteriol 185(1);115-25. PMID: 12486047

Wickner94: Wickner S, Gottesman S, Skowyra D, Hoskins J, McKenney K, Maurizi MR (1994). "A molecular chaperone, ClpA, functions like DnaK and DnaJ." Proc Natl Acad Sci U S A 91(25);12218-22. PMID: 7991609

Xia04a: Xia D, Esser L, Singh SK, Guo F, Maurizi MR (2004). "Crystallographic investigation of peptide binding sites in the N-domain of the ClpA chaperone." J Struct Biol 146(1-2);166-79. PMID: 15037248

Zeth02: Zeth K, Ravelli RB, Paal K, Cusack S, Bukau B, Dougan DA (2002). "Structural analysis of the adaptor protein ClpS in complex with the N-terminal domain of ClpA." Nat Struct Biol 2002;9(12);906-11. PMID: 12426582


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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