Escherichia coli K-12 substr. MG1655 Enzyme: oligopeptidase A

Gene: prlC Accession Numbers: EG11441 (EcoCyc), b3498, ECK3483

Synonyms: opdA

Regulation Summary Diagram: ?

Regulation summary diagram for prlC

Oligopeptidase A is a cytoplasmic protease with broad specificity. It was originally identified as a suppressor of signal sequence mutants and thus may be involved in degradation of signal peptides [Emr82, Trun87]. Oligoeptidase A appears shortly before DNA synthesis in at least some strains and may be involved in the onset of DNA replication, as treatment of cells with an inhibitor of Oligopeptidase A prevents cell division [Kato92, Irisawa93]. Oligopeptidase A may also be partially reponsible for degradation of signal peptides [Novak88].

Oligopeptidase A catalyzes broad-specificity hydrolysis of peptide bonds. In hydrolysis of bonds in signal sequence peptides, some specificity is seen for cleavage near alanine and glycine [Kato92, Irisawa93, Novak88].

Citations: [Conlin92]

Gene Citations: [Nonaka06]

Locations: cytosol

Map Position: [3,641,163 <- 3,643,205] (78.48 centisomes, 283°)
Length: 2043 bp / 680 aa

Molecular Weight of Polypeptide: 77.167 kD (from nucleotide sequence), 67 kD (experimental) [Jiang98c ]

pI: 4.9 [Kato92]

Unification Links: ASAP:ABE-0011421 , CGSC:18031 , DIP:DIP-10566N , EchoBASE:EB1411 , EcoGene:EG11441 , EcoliWiki:b3498 , EcoO157Cyc:PRLC-MONOMER , Mint:MINT-1234260 , ModBase:P27298 , OU-Microarray:b3498 , PortEco:prlC , PR:PRO_000023594 , Pride:P27298 , Protein Model Portal:P27298 , RefSeq:NP_417955 , RegulonDB:EG11441 , SMR:P27298 , String:511145.b3498 , UniProt:P27298

Relationship Links: InterPro:IN-FAMILY:IPR001567 , InterPro:IN-FAMILY:IPR024077 , InterPro:IN-FAMILY:IPR024079 , InterPro:IN-FAMILY:IPR024080 , Pfam:IN-FAMILY:PF01432 , Prosite:IN-FAMILY:PS00142

In Paralogous Gene Group: 312 (2 members)

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

GO Terms:

Biological Process: GO:0006465 - signal peptide processing Inferred from experiment [Novak88]
GO:0006260 - DNA replication Author statement [Kato92]
GO:0006508 - proteolysis Inferred by computational analysis [UniProtGOA11, GOA01]
Molecular Function: GO:0008233 - peptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Irisawa93]
GO:0004222 - metalloendopeptidase activity Inferred by computational analysis [GOA01]
GO:0008237 - metallopeptidase activity Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, Kato92]
GO:0005737 - cytoplasm Author statement [Jiang98c]

MultiFun Terms: cell processes cell division
information transfer protein related turnover, degradation
metabolism degradation of macromolecules proteins/peptides/glycopeptides

Essentiality data for prlC 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]

Revised 25-May-2011 by Brito D

Enzymatic reaction of: oligopeptidase

EC Number:

an oligopeptide + 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 direction in which it was curated.

The reaction is physiologically favored in the direction shown.

pH(opt): 9 [Kato92]

Sequence Features

Protein sequence of oligopeptidase A with features indicated

Feature Class Location Citations Comment
Sequence-Conflict 211 -> 212
[Conlin92, UniProt10a]
UniProt: (in Ref. 1; AAA16155);
Sequence-Conflict 265 -> 266
[Conlin92, UniProt10a]
UniProt: (in Ref. 1; AAA16155);
Sequence-Conflict 390
[Conlin92, UniProt10a]
UniProt: (in Ref. 1; AAA16155);
Sequence-Conflict 406
[Conlin92, UniProt10a]
UniProt: (in Ref. 1; AAA16155);
Metal-Binding-Site 469
UniProt: Zinc; catalytic; Non-Experimental Qualifier: by similarity;
Active-Site 470
UniProt: Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 473
UniProt: Zinc; catalytic; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 476
UniProt: Zinc; catalytic; Non-Experimental Qualifier: by similarity;
Sequence-Conflict 516
[Conlin92, UniProt10a]
UniProt: (in Ref. 1; AAA16155);

Gene Local Context (not to scale): ?

Gene local context diagram

Transcription Unit:

Transcription-unit diagram


10/20/97 Gene b3498 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11441; confirmed by SwissProt match.


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

Conlin92: Conlin CA, Trun NJ, Silhavy TJ, Miller CG (1992). "Escherichia coli prlC encodes an endopeptidase and is homologous to the Salmonella typhimurium opdA gene." J Bacteriol 174(18);5881-7. PMID: 1325967

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

Emr82: Emr SD, Bassford PJ (1982). "Localization and processing of outer membrane and periplasmic proteins in Escherichia coli strains harboring export-specific suppressor mutations." J Biol Chem 257(10);5852-60. PMID: 7040375

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."

Irisawa93: Irisawa T, Kato M, Moroishi J, Muramatu M (1993). "Effect of trans-4-guanidinomethylcyclohexanecarboxylic acid 4-tert-butylphenyl ester, a trypsin inhibitor, on the growth of various strains of Escherichia coli." Biol Pharm Bull 16(7);621-6. PMID: 7691339

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

Jiang98c: Jiang X, Zhang M, Ding Y, Yao J, Chen H, Zhu D, Muramatu M (1998). "Escherichia coli prlC gene encodes a trypsin-like proteinase regulating the cell cycle." J Biochem (Tokyo) 124(5);980-5. PMID: 9792922

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

Kato92: Kato M, Irisawa T, Ohtani M, Muramatu M (1992). "Purification and characterization of proteinase In, a trypsin-like proteinase, in Escherichia coli." Eur J Biochem 210(3);1007-14. PMID: 1336454

Nonaka06: Nonaka G, Blankschien M, Herman C, Gross CA, Rhodius VA (2006). "Regulon and promoter analysis of the E. coli heat-shock factor, sigma32, reveals a multifaceted cellular response to heat stress." Genes Dev 20(13);1776-89. PMID: 16818608

Novak88: Novak P, Dev IK (1988). "Degradation of a signal peptide by protease IV and oligopeptidase A." J Bacteriol 170(11);5067-75. PMID: 3053642

Trun87: Trun NJ, Silhavy TJ (1987). "Characterization and in vivo cloning of prlC, a suppressor of signal sequence mutations in Escherichia coli K12." Genetics 116(4);513-21. PMID: 2957272

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 manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Wade06: Wade JT, Roa DC, Grainger DC, Hurd D, Busby SJ, Struhl K, Nudler E (2006). "Extensive functional overlap between sigma factors in Escherichia coli." Nat Struct Mol Biol 13(9);806-14. PMID: 16892065

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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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