MetaCyc Enzyme: serine protease Do

Gene: degP Accession Numbers: EG10463 (MetaCyc), b0161, ECK0160

Synonyms: htrA, ptd, protease Do

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of serine protease Do = [DegP]6

Protease Do, or DegP, is a periplasmic serine protease required for survival at high temperatures [Lipinska89, Strauch89, Seol91]. DegP degrades abnormal proteins in the periplasm, including mutant proteins, oxidatively damaged proteins and aggregated proteins [Strauch88, Strauch89, SkorkoGlonek99, Laskowska96]. DegP has been specifically shown to degrade the mutant periplasmic protein MalS, as well as unassembled subunits from protein complexes, including HflK, LamB and PapA [Spiess99, Kihara98, Misra91, Jones02].

DegP also proteolyzes a range of other proteins that may not be quality control substrates, such as the DNA methyltransferare Ada, various forms of the colicin A lysis protein and the replication initiation inhibitor IciA [Lee90, Cavard89, Cavard95, Yoo93]. DegP also binds to the ssrA-encoded degradation tag, though this PDZ-domain-mediated interaction does not appear to allow DegP proteolysis of tagged proteins [Spiers02]. Finally, strains lacking DegP are more susceptible to the cationic antimicrobial peptide Lactoferricin B, indicating a possible role for DegP in degradation of that molecule [Ulvatne02].

DegP also has an independent chaperone activity that functions even in proteolytically inactive mutants of DegP [Spiess99]. This chaperone activity is required for survival in the case of disrupted outer membrane assembly, preventing buildup of toxic aggregates [Misra00]. There may be some redundancy between DegP and the chaperones Skp and SurA [Rizzitello01].

DegP is a six-membered ring-shaped structure with a central cavity which contains its proteolytic sites [Swamy83, Kim99a]. The hexamer is built from a pair of staggered trimeric rings, with the proteolytic cavity accessible from the sides rather than the ends [Krojer02]. There are two PDZ domains in each monomer which are required for this assembly, and which may be involved in opening and closing the lateral openings [Sassoon99]. Binding of substrate to the PDZ1 domain induces oligomer conversion from a resting hexameric state to a higher order active complex [Krojer10, Merdanovic10]. The PDZ1 domain anchors substrate, facilitating its presentation to the proteolytic domain [Krojer08]. DegP is a processive protease - cleaving its substrate into peptides with a mean size of 13-15 residues [Krojer08]. The PDZ1 domain is required for protease activity and for binding of unfolded proteins, while the PDZ2 domain is primarily required for maintaining a hexameric configuration [Iwanczyk07]. The inner cavity also has several hydrophobic patches, which may be involved in its chaperone function [Krojer02].

Hexameric DegP assembles into large catalytically active spherical structures around its substrate [Krojer08a, Jiang08]. The spherical multimers exhibit proteolytic and chaperone-like activity [Shen09b]. A model polypeptide substrate binds each DegP subunit at two sites in the crystal structure of a DegP dodecamer [Kim11d]. Substrate binding drives the formation of proteolytically active dodecamers and larger cages of 18, 24 and 30 subunits while substrate cleavage promotes cage disassembly [Kim11d].

DegP's proteolytic activity is increased at high temperatures but drops dramatically at low temperatures, leaving its chaperone function unaffected [SkorkoGlonek95, Spiess99]. DegP interacts with phosphatidylglycerol on the periplasmic face of the inner membrane, undergoing a conformational change that correlates with the temperature dependence of its proteolytic capacity [SkorkoGlonek97].

The mature form of DegP is derived by cleavage of its first twenty-six amino acids by leader peptidase [Lipinska90, Lipinska89]. Targeting of DegP to the Sec-translocase for transport across the inner membrane is SecB-dependent [Baars06].

DegP is a member of the HtrA (high temperature requirement) family of proteases which combine a protease domain with one or more PDZ domains and function as higher order oligomers [Kim05c].

DegP is downregulated during low osmolarity [Forns05].

Reviews: [Ortega09, Huber08]

Citations: [Pallen97]

Locations: inner membrane, periplasmic space

Map Position: [180,884 -> 182,308]

Molecular Weight of Polypeptide: 49.354 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000551 , CGSC:30554 , DIP:DIP-46256N , EchoBASE:EB0458 , EcoGene:EG10463 , EcoliWiki:b0161 , EcoO157Cyc:HTRA-MONOMER , Mint:MINT-1302319 , ModBase:P0C0V0 , OU-Microarray:b0161 , PortEco:degP , PR:PRO_000022425 , Pride:P0C0V0 , Protein Model Portal:P0C0V0 , RefSeq:NP_414703 , RegulonDB:EG10463 , SMR:P0C0V0 , String:511145.b0161 , Swiss-Model:P0C0V0 , UniProt:P0C0V0

Relationship Links: InterPro:IN-FAMILY:IPR001478 , InterPro:IN-FAMILY:IPR001940 , InterPro:IN-FAMILY:IPR009003 , InterPro:IN-FAMILY:IPR011782 , PDB:Structure:1KY9 , PDB:Structure:2ZLE , PDB:Structure:3CS0 , PDB:Structure:3MH4 , PDB:Structure:3MH5 , PDB:Structure:3MH6 , PDB:Structure:3MH7 , PDB:Structure:3OTP , PDB:Structure:3OU0 , PDB:Structure:4A8D , Pfam:IN-FAMILY:PF00595 , Prints:IN-FAMILY:PR00834 , Prosite:IN-FAMILY:PS50106 , Smart:IN-FAMILY:SM00228

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006457 - protein folding Inferred from experiment [Spiess99]
GO:0006508 - proteolysis Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Lipinska90]
GO:0006515 - misfolded or incompletely synthesized protein catabolic process Inferred from experiment [Spiess99]
GO:0006979 - response to oxidative stress Inferred from experiment [SkorkoGlonek99]
GO:0009266 - response to temperature stimulus Inferred from experiment [Spiess99]
Molecular Function: GO:0004252 - serine-type endopeptidase activity Inferred from experiment Inferred by computational analysis [GOA01a, Lipinska90, Shen09b]
GO:0005515 - protein binding Inferred from experiment [Ge14, Kim11d]
GO:0042802 - identical protein binding Inferred from experiment [Kim11d]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0008233 - peptidase activity Inferred by computational analysis [UniProtGOA11a]
GO:0008236 - serine-type peptidase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment [SkorkoGlonek99, Strauch88]
GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]

MultiFun Terms: cell processes adaptations other (mechanical, nutritional, oxidative stress)
cell processes adaptations temperature extremes
information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides

Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

Enzymatic reaction of: serine protease

EC Number: 3.4.21.-

a polypeptide[periplasmic space] + H2O[periplasmic space] <=> 2 a polypeptide[periplasmic space]

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

The reaction is physiologically favored in the direction shown.

Imported from EcoCyc 27-Jan-2015 by Paley S , SRI International

T(opt): 55 °C [BRENDA14, SkorkoGlonek95]

pH(opt): 7.6 [BRENDA14, Jiang08]

Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 26
[Lipinska90, Lipinska89]
Sequence-Conflict 10
[Wurgler90, Lipinska88, UniProt10a]
UniProt: (in Ref. 1 and 7);
Chain 27 -> 474
UniProt: Protease do;
Sequence-Conflict 46
[Quirk90, UniProt10a]
UniProt: (in Ref. 6; AAA23717);
Amino-Acid-Sites-That-Bind 58
UniProt: Substrate.
Disulfide-Bond-Site 83, 95
[SkorkoGlonek03, UniProt11]
Mutagenesis-Variant 131
[SkorkoGlonek95a, UniProt12a]
UniProt: Loss of peptidase activity with no detectable changes in secondary structure.
Amino-Acid-Sites-That-Bind 131
UniProt: Substrate.
Active-Site 131
UniProt: Charge relay system.
Amino-Acid-Sites-That-Bind 161
UniProt: Substrate.
Active-Site 161
UniProt: Charge relay system; Non-Experimental Qualifier: potential;
Sequence-Conflict 192
[Lipinska88, UniProt10a]
UniProt: (in Ref. 1; AAA23994/CAA30997);
Protein-Segment 234 -> 236
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 236
[Pan03, SkorkoGlonek95a, UniProt12a]
UniProt: Loss of peptidase activity with no detectable changes in secondary structure.
Active-Site 236
UniProt: Charge relay system.
Protein-Segment 252 -> 256
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Mutagenesis-Variant 254
[SobieckaSzkatul10, UniProt12a]
UniProt: It does not affect the proteolytic activity.
Mutagenesis-Variant 255
[SobieckaSzkatul10, UniProt12a]
UniProt: Loss of proteolytic activity.
Mutagenesis-Variant 258
[SobieckaSzkatul10, UniProt12a]
UniProt: Increases the proteolytic activity.
Mutagenesis-Variant 261
[SobieckaSzkatul10, UniProt12a]
UniProt: Loss of proteolytic activity.
Mutagenesis-Variant 262
[SobieckaSzkatul10, UniProt12a]
UniProt: Stimulates the proteolytic activity at low temperatures (20-30 degrees Celsius), whereas at higher temperatures (above 35 degrees Celsius), the proteolytic activity is less efficient.
Mutagenesis-Variant 264
[SobieckaSzkatul10, UniProt12a]
UniProt: Loss of proteolytic activity.
Conserved-Region 280 -> 371
UniProt: PDZ 1;
Protein-Segment 291 -> 295
UniProt: Substrate binding; Sequence Annotation Type: region of interest.
Conserved-Region 377 -> 466
UniProt: PDZ 2;
Sequence-Conflict 467 -> 474
[Lipinska88, UniProt10a]
UniProt: (in Ref. 1; AAA23994/CAA30997);

10/20/97 Gene b0161 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10463; confirmed by SwissProt match.


Baars06: Baars L, Ytterberg AJ, Drew D, Wagner S, Thilo C, van Wijk KJ, de Gier JW (2006). "Defining the role of the Escherichia coli chaperone SecB using comparative proteomics." J Biol Chem 281(15);10024-34. PMID: 16352602

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014."

Cavard89: Cavard D, Lazdunski C, Howard SP (1989). "The acylated precursor form of the colicin A lysis protein is a natural substrate of the DegP protease." J Bacteriol 171(11);6316-22. PMID: 2681163

Cavard95: Cavard D (1995). "Role of DegP protease on levels of various forms of colicin A lysis protein." FEMS Microbiol Lett 125(2-3);173-8. PMID: 7875565

Forns05: Forns N, Juarez A, Madrid C (2005). "Osmoregulation of the HtrA (DegP) protease of Escherichia coli: an Hha-H-NS complex represses HtrA expression at low osmolarity." FEMS Microbiol Lett 251(1);75-80. PMID: 16143461

Ge14: Ge X, Wang R, Ma J, Liu Y, Ezemaduka AN, Chen PR, Fu X, Chang Z (2014). "DegP primarily functions as a protease for the biogenesis of β-barrel outer membrane proteins in the Gram-negative bacterium Escherichia coli." FEBS J 281(4):1226-1240. PMID: 24373465

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

Huber08: Huber D, Bukau B (2008). "DegP: a Protein "Death Star"." Structure 16(7);989-90. PMID: 18611371

Iwanczyk07: Iwanczyk J, Damjanovic D, Kooistra J, Leong V, Jomaa A, Ghirlando R, Ortega J (2007). "Role of the PDZ domains in Escherichia coli DegP protein." J Bacteriol 189(8);3176-86. PMID: 17277057

Jiang08: Jiang J, Zhang X, Chen Y, Wu Y, Zhou ZH, Chang Z, Sui SF (2008). "Activation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins." Proc Natl Acad Sci U S A 105(33);11939-44. PMID: 18697939

Jones02: Jones CH, Dexter P, Evans AK, Liu C, Hultgren SJ, Hruby DE (2002). "Escherichia coli DegP protease cleaves between paired hydrophobic residues in a natural substrate: the PapA pilin." J Bacteriol 184(20);5762-71. PMID: 12270835

Kihara98: Kihara A, Ito K (1998). "Translocation, folding, and stability of the HflKC complex with signal anchor topogenic sequences." J Biol Chem 273(45);29770-5. PMID: 9792691

Kim05c: Kim DY, Kim KK (2005). "Structure and function of HtrA family proteins, the key players in protein quality control." J Biochem Mol Biol 38(3);266-74. PMID: 15943900

Kim11d: Kim S, Grant RA, Sauer RT (2011). "Covalent linkage of distinct substrate degrons controls assembly and disassembly of DegP proteolytic cages." Cell 145(1);67-78. PMID: 21458668

Kim99a: Kim KI, Park SC, Kang SH, Cheong GW, Chung CH (1999). "Selective degradation of unfolded proteins by the self-compartmentalizing HtrA protease, a periplasmic heat shock protein in Escherichia coli." J Mol Biol 294(5);1363-74. PMID: 10600391

Krojer02: Krojer T, Garrido-Franco M, Huber R, Ehrmann M, Clausen T (2002). "Crystal structure of DegP (HtrA) reveals a new protease-chaperone machine." Nature 416(6879);455-9. PMID: 11919638

Krojer08: Krojer T, Pangerl K, Kurt J, Sawa J, Stingl C, Mechtler K, Huber R, Ehrmann M, Clausen T (2008). "Interplay of PDZ and protease domain of DegP ensures efficient elimination of misfolded proteins." Proc Natl Acad Sci U S A 105(22);7702-7. PMID: 18505836

Krojer08a: Krojer T, Sawa J, Schafer E, Saibil HR, Ehrmann M, Clausen T (2008). "Structural basis for the regulated protease and chaperone function of DegP." Nature 453(7197);885-90. PMID: 18496527

Krojer10: Krojer T, Sawa J, Huber R, Clausen T (2010). "HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues." Nat Struct Mol Biol 17(7);844-52. PMID: 20581825

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

Lee90: Lee CS, Hahm JK, Hwang BJ, Park KC, Ha DB, Park SD, Chung CH (1990). "Processing of Ada protein by two serine endoproteases Do and So from Escherichia coli." FEBS Lett 262(2);310-2. PMID: 2159417

Lipinska88: Lipinska B, Sharma S, Georgopoulos C (1988). "Sequence analysis and regulation of the htrA gene of Escherichia coli: a sigma 32-independent mechanism of heat-inducible transcription." Nucleic Acids Res 16(21);10053-67. PMID: 3057437

Lipinska89: Lipinska B, Fayet O, Baird L, Georgopoulos C (1989). "Identification, characterization, and mapping of the Escherichia coli htrA gene, whose product is essential for bacterial growth only at elevated temperatures." J Bacteriol 171(3);1574-84. PMID: 2537822

Lipinska90: Lipinska B, Zylicz M, Georgopoulos C (1990). "The HtrA (DegP) protein, essential for Escherichia coli survival at high temperatures, is an endopeptidase." J Bacteriol 172(4);1791-7. PMID: 2180903

Merdanovic10: Merdanovic M, Mamant N, Meltzer M, Poepsel S, Auckenthaler A, Melgaard R, Hauske P, Nagel-Steger L, Clarke AR, Kaiser M, Huber R, Ehrmann M (2010). "Determinants of structural and functional plasticity of a widely conserved protease chaperone complex." Nat Struct Mol Biol 17(7);837-43. PMID: 20581826

Misra00: Misra R, CastilloKeller M, Deng M (2000). "Overexpression of protease-deficient DegP(S210A) rescues the lethal phenotype of Escherichia coli OmpF assembly mutants in a degP background." J Bacteriol 182(17);4882-8. PMID: 10940032

Misra91: Misra R, Peterson A, Ferenci T, Silhavy TJ (1991). "A genetic approach for analyzing the pathway of LamB assembly into the outer membrane of Escherichia coli." J Biol Chem 266(21);13592-7. PMID: 1856196

Ortega09: Ortega J, Iwanczyk J, Jomaa A (2009). "Escherichia coli DegP: a structure-driven functional model." J Bacteriol 191(15);4705-13. PMID: 19465652

Pallen97: Pallen MJ, Wren BW (1997). "The HtrA family of serine proteases." Mol Microbiol 26(2);209-21. PMID: 9383148

Pan03: Pan KL, Hsiao HC, Weng CL, Wu MS, Chou CP (2003). "Roles of DegP in prevention of protein misfolding in the periplasm upon overexpression of penicillin acylase in Escherichia coli." J Bacteriol 185(10);3020-30. PMID: 12730160

Quirk90: Quirk S, Bhatnagar SK, Bessman MJ (1990). "Primary structure of the deoxyguanosine triphosphate triphosphohydrolase-encoding gene (dgt) of Escherichia coli." Gene 1990;89(1);13-8. PMID: 2165018

Rizzitello01: Rizzitello AE, Harper JR, Silhavy TJ (2001). "Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli." J Bacteriol 183(23);6794-800. PMID: 11698367

Sassoon99: Sassoon N, Arie JP, Betton JM (1999). "PDZ domains determine the native oligomeric structure of the DegP (HtrA) protease." Mol Microbiol 33(3);583-9. PMID: 10417648

Seol91: Seol JH, Woo SK, Jung EM, Yoo SJ, Lee CS, Kim KJ, Tanaka K, Ichihara A, Ha DB, Chung CH (1991). "Protease Do is essential for survival of Escherichia coli at high temperatures: its identity with the htrA gene product." Biochem Biophys Res Commun 176(2);730-6. PMID: 2025286

Shen09b: Shen QT, Bai XC, Chang LF, Wu Y, Wang HW, Sui SF (2009). "Bowl-shaped oligomeric structures on membranes as DegP's new functional forms in protein quality control." Proc Natl Acad Sci U S A 106(12);4858-63. PMID: 19255437

SkorkoGlonek03: Skorko-Glonek J, Zurawa D, Tanfani F, Scire A, Wawrzynow A, Narkiewicz J, Bertoli E, Lipinska B (2003). "The N-terminal region of HtrA heat shock protease from Escherichia coli is essential for stabilization of HtrA primary structure and maintaining of its oligomeric structure." Biochim Biophys Acta 1649(2);171-82. PMID: 12878036

SkorkoGlonek95: Skorko-Glonek J, Krzewski K, Lipinska B, Bertoli E, Tanfani F (1995). "Comparison of the structure of wild-type HtrA heat shock protease and mutant HtrA proteins. A Fourier transform infrared spectroscopic study." J Biol Chem 270(19);11140-6. PMID: 7744744

SkorkoGlonek95a: Skorko-Glonek J, Wawrzynow A, Krzewski K, Kurpierz K, Lipinska B (1995). "Site-directed mutagenesis of the HtrA (DegP) serine protease, whose proteolytic activity is indispensable for Escherichia coli survival at elevated temperatures." Gene 163(1);47-52. PMID: 7557477

SkorkoGlonek97: Skorko-Glonek J, Lipinska B, Krzewski K, Zolese G, Bertoli E, Tanfani F (1997). "HtrA heat shock protease interacts with phospholipid membranes and undergoes conformational changes." J Biol Chem 272(14);8974-82. PMID: 9083020

SkorkoGlonek99: Skorko-Glonek J, Zurawa D, Kuczwara E, Wozniak M, Wypych Z, Lipinska B (1999). "The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress." Mol Gen Genet 262(2);342-50. PMID: 10517331

SobieckaSzkatul10: Sobiecka-Szkatula A, Gieldon A, Scire A, Tanfani F, Figaj D, Koper T, Ciarkowski J, Lipinska B, Skorko-Glonek J (2010). "The role of the L2 loop in the regulation and maintaining the proteolytic activity of HtrA (DegP) protein from Escherichia coli." Arch Biochem Biophys 500(2);123-30. PMID: 20515644

Spiers02: Spiers A, Lamb HK, Cocklin S, Wheeler KA, Budworth J, Dodds AL, Pallen MJ, Maskell DJ, Charles IG, Hawkins AR (2002). "PDZ domains facilitate binding of high temperature requirement protease A (HtrA) and tail-specific protease (Tsp) to heterologous substrates through recognition of the small stable RNA A (ssrA)-encoded peptide." J Biol Chem 277(42);39443-9. PMID: 12177052

Spiess99: Spiess C, Beil A, Ehrmann M (1999). "A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein." Cell 97(3);339-47. PMID: 10319814

Strauch88: Strauch KL, Beckwith J (1988). "An Escherichia coli mutation preventing degradation of abnormal periplasmic proteins." Proc Natl Acad Sci U S A 85(5);1576-80. PMID: 3278319

Strauch89: Strauch KL, Johnson K, Beckwith J (1989). "Characterization of degP, a gene required for proteolysis in the cell envelope and essential for growth of Escherichia coli at high temperature." J Bacteriol 171(5);2689-96. PMID: 2540154

Swamy83: Swamy KH, Chung CH, Goldberg AL (1983). "Isolation and characterization of protease do from Escherichia coli, a large serine protease containing multiple subunits." Arch Biochem Biophys 224(2);543-54. PMID: 6347072

Ulvatne02: Ulvatne H, Haukland HH, Samuelsen O, Kramer M, Vorland LH (2002). "Proteases in Escherichia coli and Staphylococcus aureus confer reduced susceptibility to lactoferricin B." J Antimicrob Chemother 50(4);461-7. PMID: 12356789

UniProt09: UniProt Consortium (2009). "UniProt version 15.8 released on 2009-10-01 00:00:00." Database.

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.

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

UniProt11a: UniProt Consortium (2011). "UniProt version 2011-11 released on 2011-11-22 00:00:00." Database.

UniProt12a: UniProt Consortium (2012). "UniProt version 2012-02 released on 2012-02-29 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."

Wurgler90: Wurgler SM, Richardson CC (1990). "Structure and regulation of the gene for dGTP triphosphohydrolase from Escherichia coli." Proc Natl Acad Sci U S A 87(7);2740-4. PMID: 2157212

Yoo93: Yoo SJ, Seol JH, Woo SK, Suh SW, Hwang DS, Ha DB, Chung CH (1993). "Hydrolysis of the IciA protein, an inhibitor of DNA replication initiation, by protease Do in Escherichia coli." FEBS Lett 327(1);17-20. PMID: 8335089

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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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