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MetaCyc Enzyme: protease III

Gene: ptrA Accession Numbers: EG10786 (MetaCyc), b2821, ECK2817

Synonyms: ptr, Pitrilysin, Protease pi

Species: Escherichia coli K-12 substr. MG1655

Summary:
Protease III is a periplasmic protein that rapidly degrades small proteins and peptides in vitro [Swamy82, Cheng79, Cornista04, Anastasi93]. Protease III is partially responsible for degrading A-β-lactamase as well as misfolded MalE31 [Baneyx91, Betton98].

Protease III is a zinc metalloendopeptidase with a nontraditional zinc-binding motif, featuring the consensus sequence HXXEH rather than the more traditional HEXXH [Ding92, Becker92]. In addition to the two histidines in the zinc-binding motif, glutamate162 is also required for zinc coordination [Becker93].

A 50 kDa polypeptide with no apparent protease function derived from the N-terminal end of protease III can be found in the periplasm under some circumstances [Dykstra85].

Citations: [Anastasi95, Becker95]

Locations: periplasmic space, cytosol

Map Position: [2,954,018 <- 2,956,906]

Molecular Weight of Polypeptide: 107.71 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0009252 , CGSC:351 , EchoBASE:EB0779 , EcoGene:EG10786 , EcoliWiki:b2821 , EcoO157Cyc:PTR-MONOMER , ModBase:P05458 , OU-Microarray:b2821 , PortEco:ptrA , PR:PRO_000023629 , Pride:P05458 , Protein Model Portal:P05458 , RefSeq:NP_417298 , RegulonDB:EG10786 , SMR:P05458 , String:511145.b2821 , UniProt:P05458

Relationship Links: InterPro:IN-FAMILY:IPR001431 , InterPro:IN-FAMILY:IPR007863 , InterPro:IN-FAMILY:IPR011237 , InterPro:IN-FAMILY:IPR011249 , InterPro:IN-FAMILY:IPR011765 , PDB:Structure:1Q2L , Pfam:IN-FAMILY:PF00675 , Pfam:IN-FAMILY:PF05193 , Prosite:IN-FAMILY:PS00143

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA01a, Cheng79, Swamy82]
Molecular Function: GO:0004222 - metalloendopeptidase activity Inferred from experiment Inferred by computational analysis [GOA01a, Cheng79]
GO:0008237 - metallopeptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11a, Ding92]
GO:0008270 - zinc ion binding Inferred from experiment [Ding92]
GO:0003824 - catalytic activity Inferred by computational analysis [GOA01a]
GO:0008233 - peptidase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a, GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred from experiment [Cheng79]
GO:0030288 - outer membrane-bounded periplasmic space Inferred from experiment Inferred by computational analysis [DiazMejia09, Han13, LopezCampistrou05, Swamy82]
GO:0042597 - periplasmic space Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]

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

Credits:
Revised in EcoCyc 25-May-2011 by Weerasinghe D
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: protease

EC Number: 3.4.24.55

a protein + H2O <=> n 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

T(opt): 45 °C [BRENDA14, Fricke95a]

pH(opt): 7.5 [BRENDA14, Anastasi95]


Sequence Features

Feature Class Location Citations Comment
Signal-Sequence 1 -> 23
[UniProt10a]
Chain 24 -> 962
[UniProt09]
UniProt: Protease 3;
Metal-Binding-Site 88
[Becker92, UniProt11]
UniProt: Zinc.
Mutagenesis-Variant 88
[UniProt10a]
Alternate sequence: R; UniProt: Loss of activity and of Zn-binding;
Active-Site 91
[Becker93, Becker92, UniProt11]
UniProt: Proton acceptor.
Mutagenesis-Variant 91
[UniProt10a]
Alternate sequence: Q; UniProt: Loss of activity;
Metal-Binding-Site 92
[Becker92, UniProt11]
UniProt: Zinc.
Mutagenesis-Variant 92
[UniProt10a]
Alternate sequence: R; UniProt: Loss of activity and of Zn-binding;
Mutagenesis-Variant 162
[UniProt10a]
Alternate sequence: Q; UniProt: 20% loss of activity;
Mutagenesis-Variant 169
[UniProt10a]
Alternate sequence: Q; UniProt: Loss of activity and of Zn-binding;
Metal-Binding-Site 169
[UniProt10a]
UniProt: Zinc;
Mutagenesis-Variant 204
[UniProt10a]
Alternate sequence: Q; UniProt: No loss of activity;
Sequence-Conflict 277 -> 284
[ClaverieMartin87, UniProt10a]
Alternate sequence: HYHSLRPW; UniProt: (in Ref. 5; AAA24436);

History:
10/20/97 Gene b2821 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10786; confirmed by SwissProt match.


References

Anastasi93: Anastasi A, Knight CG, Barrett AJ (1993). "Characterization of the bacterial metalloendopeptidase pitrilysin by use of a continuous fluorescence assay." Biochem J 290 ( Pt 2);601-7. PMID: 7680857

Anastasi95: Anastasi A, Barrett AJ (1995). "Pitrilysin." Methods Enzymol 248;684-92. PMID: 7674955

Baneyx91: Baneyx F, Georgiou G (1991). "Construction and characterization of Escherichia coli strains deficient in multiple secreted proteases: protease III degrades high-molecular-weight substrates in vivo." J Bacteriol 173(8);2696-703. PMID: 2013581

Becker92: Becker AB, Roth RA (1992). "An unusual active site identified in a family of zinc metalloendopeptidases." Proc Natl Acad Sci U S A 89(9);3835-9. PMID: 1570301

Becker93: Becker AB, Roth RA (1993). "Identification of glutamate-169 as the third zinc-binding residue in proteinase III, a member of the family of insulin-degrading enzymes." Biochem J 292 ( Pt 1);137-42. PMID: 8099278

Becker95: Becker AB, Roth RA (1995). "Insulysin and pitrilysin: insulin-degrading enzymes of mammals and bacteria." Methods Enzymol 248;693-703. PMID: 7674956

Betton98: Betton JM, Sassoon N, Hofnung M, Laurent M (1998). "Degradation versus aggregation of misfolded maltose-binding protein in the periplasm of Escherichia coli." J Biol Chem 273(15);8897-902. PMID: 9535871

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

Cheng79: Cheng YS, Zipser D (1979). "Purification and characterization of protease III from Escherichia coli." J Biol Chem 254(11);4698-706. PMID: 374413

ClaverieMartin87: Claverie-Martin F, Diaz-Torres MR, Kushner SR (1987). "Analysis of the regulatory region of the protease III (ptr) gene of Escherichia coli K-12." Gene 54(2-3);185-95. PMID: 3308636

Cornista04: Cornista J, Ikeuchi S, Haruki M, Kohara A, Takano K, Morikawa M, Kanaya S (2004). "Cleavage of various peptides with pitrilysin from Escherichia coli: kinetic analyses using beta-endorphin and its derivatives." Biosci Biotechnol Biochem 68(10);2128-37. PMID: 15502359

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

Ding92: Ding L, Becker AB, Suzuki A, Roth RA (1992). "Comparison of the enzymatic and biochemical properties of human insulin-degrading enzyme and Escherichia coli protease III." J Biol Chem 267(4);2414-20. PMID: 1733942

Dykstra85: Dykstra CC, Kushner SR (1985). "Physical characterization of the cloned protease III gene from Escherichia coli K-12." J Bacteriol 163(3);1055-9. PMID: 2993229

Fricke95a: Fricke B, Betz R, Friebe S (1995). "A periplasmic insulin-cleaving proteinase (ICP) from Acinetobacter calcoaceticus sharing properties with protease III from Escherichia coli and IDE from eucaryotes." J Basic Microbiol 35(1);21-31. PMID: 7738784

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

Han13: Han MJ, Kim JY, Kim JA (2013). "Comparison of the large-scale periplasmic proteomes of the Escherichia coli K-12 and B strains." J Biosci Bioeng. PMID: 24140104

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

Swamy82: Swamy KH, Goldberg AL (1982). "Subcellular distribution of various proteases in Escherichia coli." J Bacteriol 149(3);1027-33. PMID: 7037737

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

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."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Thu Nov 27, 2014, BIOCYC14A.