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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites MAYBE down
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Escherichia coli K-12 substr. MG1655 Enzyme: peptidase T



Gene: pepT Accession Numbers: EG11549 (EcoCyc), b1127, ECK1113

Synonyms: aminotripeptidase, tripeptide aminopeptidase

Regulation Summary Diagram: ?

Subunit composition of peptidase T = [PepT]2
         peptidase T = PepT

Summary:
Peptidase T is a tripeptidase that can cleave the amino-terminal leucine, lysine, methionine or phenylalanine residue from certain tripeptides [Sussman70, Simmonds76, Hermsdorf78].

Expression of PepT is upregulated during biofilm development and anaerobic growth [PrigentCombaret99].

A crystal structure of PepT has been solved [Badger05].

Citations: [Lombardo93]

Locations: cytosol

Map Position: [1,185,067 -> 1,186,293] (25.54 centisomes)
Length: 1227 bp / 408 aa

Molecular Weight of Polypeptide: 44.923 kD (from nucleotide sequence)

Molecular Weight of Multimer: 80.0 kD (experimental) [Hermsdorf78]

Unification Links: ASAP:ABE-0003800 , CGSC:31914 , DIP:DIP-10461N , EchoBASE:EB1511 , EcoGene:EG11549 , EcoliWiki:b1127 , Mint:MINT-1219063 , ModBase:P29745 , OU-Microarray:b1127 , PortEco:pepT , PR:PRO_000023512 , Pride:P29745 , Protein Model Portal:P29745 , RefSeq:NP_415645 , RegulonDB:EG11549 , SMR:P29745 , String:511145.b1127 , Swiss-Model:P29745 , UniProt:P29745

Relationship Links: InterPro:IN-FAMILY:IPR001261 , InterPro:IN-FAMILY:IPR002933 , InterPro:IN-FAMILY:IPR010161 , InterPro:IN-FAMILY:IPR011650 , PDB:Structure:1VIX , Pfam:IN-FAMILY:PF01546 , Pfam:IN-FAMILY:PF07687 , Prosite:IN-FAMILY:PS00758 , Prosite:IN-FAMILY:PS00759

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006518 - peptide metabolic process Inferred from experiment Inferred by computational analysis [GOA01a, Sussman70]
GO:0006508 - proteolysis Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14, Butland05]
GO:0042803 - protein homodimerization activity Inferred from experiment [Hermsdorf78]
GO:0045148 - tripeptide aminopeptidase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Hermsdorf78]
GO:0004177 - aminopeptidase activity Inferred by computational analysis [UniProtGOA11a]
GO:0008233 - peptidase activity Inferred by computational analysis [UniProtGOA11a]
GO:0008237 - metallopeptidase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA06, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]

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

Essentiality data for pepT 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:
Last-Curated ? 27-Feb-2014 by Keseler I , SRI International


Enzymatic reaction of: tripeptide aminopeptidase (peptidase T)

EC Number: 3.4.11.4

a tripeptide + H2O <=> a dipeptide + a standard α amino acid

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

The reaction is physiologically favored in the direction shown.

Summary:
The apparent Km for methionylglycylglycine is 5.3 mM [Hermsdorf78].

pH(opt): 8.5 [Hermsdorf78]


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 78
[UniProt10]
UniProt: Zinc 1;
Active-Site 80
[UniProt10a]
UniProt: Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 140
[UniProt10]
UniProt: Zinc 1;
Active-Site 173
[UniProt10a]
UniProt: Proton acceptor; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 174
[UniProt10]
UniProt: Zinc 2;
Metal-Binding-Site 196
[UniProt10]
UniProt: Zinc 1;
Metal-Binding-Site 379
[UniProt10]
UniProt: Zinc 2;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1127 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11549; confirmed by SwissProt match.


References

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

Badger05: Badger J, Sauder JM, Adams JM, Antonysamy S, Bain K, Bergseid MG, Buchanan SG, Buchanan MD, Batiyenko Y, Christopher JA, Emtage S, Eroshkina A, Feil I, Furlong EB, Gajiwala KS, Gao X, He D, Hendle J, Huber A, Hoda K, Kearins P, Kissinger C, Laubert B, Lewis HA, Lin J, Loomis K, Lorimer D, Louie G, Maletic M, Marsh CD, Miller I, Molinari J, Muller-Dieckmann HJ, Newman JM, Noland BW, Pagarigan B, Park F, Peat TS, Post KW, Radojicic S, Ramos A, Romero R, Rutter ME, Sanderson WE, Schwinn KD, Tresser J, Winhoven J, Wright TA, Wu L, Xu J, Harris TJ (2005). "Structural analysis of a set of proteins resulting from a bacterial genomics project." Proteins 60(4);787-96. PMID: 16021622

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

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

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, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: 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."

Hermsdorf78: Hermsdorf CL (1978). "Tripeptide-specific aminopeptidase from Escherichia coli AJ005." Biochemistry 17(16);3370-6. PMID: 356879

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

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

Lombardo93: Lombardo MJ, Miller CG, Rudd KE (1993). "Physical mapping of the Escherichia coli pepT and potABCD genes." J Bacteriol 1993;175(23);7745-6. PMID: 8244951

PrigentCombaret99: Prigent-Combaret C, Vidal O, Dorel C, Lejeune P (1999). "Abiotic surface sensing and biofilm-dependent regulation of gene expression in Escherichia coli." J Bacteriol 181(19);5993-6002. PMID: 10498711

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

Simmonds76: Simmonds S, Szeto KS, Fletterick CG (1976). "Soluble tri- and dipeptidases in Escherichia coli K-12+." Biochemistry 15(2);261-71. PMID: 764862

Sussman70: Sussman AJ, Gilvarg C (1970). "Peptidases in Escherichia coli K-12 capable of cleaving lysine homopeptides." J Biol Chem 245(24);6518-24. PMID: 4991642

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 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."

Other References Related to Gene Regulation

Constantinidou06: Constantinidou C, Hobman JL, Griffiths L, Patel MD, Penn CW, Cole JA, Overton TW (2006). "A reassessment of the FNR regulon and transcriptomic analysis of the effects of nitrate, nitrite, NarXL, and NarQP as Escherichia coli K12 adapts from aerobic to anaerobic growth." J Biol Chem 281(8);4802-15. PMID: 16377617

MendozaVargas09: Mendoza-Vargas A, Olvera L, Olvera M, Grande R, Vega-Alvarado L, Taboada B, Jimenez-Jacinto V, Salgado H, Juarez K, Contreras-Moreira B, Huerta AM, Collado-Vides J, Morett E (2009). "Genome-wide identification of transcription start sites, promoters and transcription factor binding sites in E. coli." PLoS One 4(10);e7526. PMID: 19838305


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 25, 2014, BIOCYC13A.