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Escherichia coli K-12 substr. MG1655 Enzyme: outer membrane metallopeptidase



Gene: loiP Accession Numbers: EG11291 (EcoCyc), b2936, ECK2931

Synonyms: yggG

Regulation Summary Diagram: ?

Summary:
LoiP is an outer membrane metalloprotease that preferentially cleaves between Phe/Phe residues [Lutticke12]

LoiP is predicted to be a lipoprotein with a type II signal peptide [Gonnet04]. The protein is associated with the membrane fraction [Huang08a]. LoiP is an outer membrane lipoprotein [Lutticke12]. LoiP has one intramolecular S-S bond plus one additional cysteine that mediates lipid attachment [Lutticke12].|

Expression of loiP is upregulated in response to stress (heat shock, UV irradiation) and in an era-1 mutant background [Huang07b, Huang08a]. loiP is upregulated and increased amounts of LoiP are produced when cells are grown in low osmolarity media [Lutticke12]. Overexpression of full-length loiP inhibits growth [Huang08a]. There is no significant difference in growth between wild-type and a loiP deletion strain when grown in low osmolarity media [Lutticke12].

LoiP and YfgC interact and LoiP is not detected in the outer membrane of a yfgC null mutant (tested at 42oC in rich media containing 0.5M NaCl) [Lutticke12].

LoiP interacts directly with Era, an essential GTPase [Huang07b]. LoiP appears to enhance expression of agmatinase [Szumanski92]. loiP may be a member of the Rcs regulon [Hagiwara03].

LoiP: "low osmolarity induced protease" [Lutticke12]

Locations: outer membrane

Map Position: [3,079,935 -> 3,080,693] (66.38 centisomes)
Length: 759 bp / 252 aa

Molecular Weight of Polypeptide: 26.842 kD (from nucleotide sequence), 25.0 kD (experimental) [Huang07b ]

Unification Links: ASAP:ABE-0009629 , DIP:DIP-12186N , EchoBASE:EB1268 , EcoGene:EG11291 , EcoliWiki:b2936 , Mint:MINT-1288575 , OU-Microarray:b2936 , PortEco:yggG , Pride:P25894 , Protein Model Portal:P25894 , RefSeq:NP_417411 , RegulonDB:EG11291 , SMR:P25894 , String:511145.b2936 , UniProt:P25894

Relationship Links: InterPro:IN-FAMILY:IPR001915 , Pfam:IN-FAMILY:PF01435 , Prosite:IN-FAMILY:PS51257

In Paralogous Gene Group: 422 (3 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006508 - proteolysis Inferred by computational analysis [UniProtGOA11, GOA01]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
Molecular Function: GO:0008237 - metallopeptidase activity Inferred from experiment Inferred by computational analysis [UniProtGOA11, Lutticke12]
GO:0004222 - metalloendopeptidase activity Inferred by computational analysis [GOA01]
GO:0008233 - peptidase activity Inferred by computational analysis [UniProtGOA11]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0009279 - cell outer membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Lutticke12]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01, Huang08a]

Gene Class: ORFs Conserved-ORFs

Essentiality data for loiP 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:
Curated 07-Nov-2007 by Keseler I , SRI International
Last-Curated ? 24-May-2012 by Mackie A , Macquarie University


Enzymatic reaction of: metalloppeptidase (outer membrane metallopeptidase)

EC Number: 3.4.24.-

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 direction in which it was curated.

The reaction is physiologically favored in the direction shown.


Sequence Features

Feature Class Location Common Name Citations Comment
Signal-Sequence 1 -> 18 predicted type II signal peptide
[Gonnet04]
 
Lipid-Binding-Site 19  
[UniProt13]
UniProt: N-palmitoyl cysteine; Non-Experimental Qualifier: potential.
Chain 19 -> 252  
[UniProt13]
UniProt: Metalloprotease LoiP.
Disulfide-Bond-Site 108, 53  
[Lutticke12, UniProt13]
Metal-Binding-Site 130  
[UniProt10a]
UniProt: Zinc; catalytic; Non-Experimental Qualifier: potential;
Active-Site 131  
[UniProt10a]
UniProt: Non-Experimental Qualifier: potential;
Metal-Binding-Site 134  
[UniProt10a]
UniProt: Zinc; catalytic; Non-Experimental Qualifier: potential;
Metal-Binding-Site 189  
[UniProt10a]
UniProt: Zinc; catalytic; Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Peter D. Karp on Wed Jan 18, 2006:
Gene left-end position adjusted based on analysis performed in the 2005 E. coli annotation update [Riley06 ].
Peter D. Karp on Thu Jan 16, 2003:
Predicted gene function revised as a result of E. coli genome reannotation by Serres et al. [Serres01 ].
10/20/97 Gene b2936 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG11291; 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

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."

Gonnet04: Gonnet P, Rudd KE, Lisacek F (2004). "Fine-tuning the prediction of sequences cleaved by signal peptidase II: a curated set of proven and predicted lipoproteins of Escherichia coli K-12." Proteomics 4(6);1597-613. PMID: 15174130

Hagiwara03: Hagiwara D, Sugiura M, Oshima T, Mori H, Aiba H, Yamashino T, Mizuno T (2003). "Genome-wide analyses revealing a signaling network of the RcsC-YojN-RcsB phosphorelay system in Escherichia coli." J Bacteriol 185(19);5735-46. PMID: 13129944

Huang07b: Huang Y, Zhang B, Dong K, Zhang X, Hou L, Wang T, Chen N, Chen S (2007). "Up-regulation of yggG promotes the survival of Escherichia coli cells containing Era-1 mutant protein." FEMS Microbiol Lett 275(1):8-15. PMID: 17651431

Huang08a: Huang Y, Dong K, Zhang X, Zhang B, Hou L, Chen N, Chen S (2008). "Expression and Regulation of the yggG Gene of Escherichia coli." Curr Microbiol 56(1):14-20. PMID: 17909889

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

Lutticke12: Lutticke C, Hauske P, Lewandrowski U, Sickmann A, Kaiser M, Ehrmann M (2012). "E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds." Mol Biosyst 8(6);1775-82. PMID: 22491786

Riley06: Riley M, Abe T, Arnaud MB, Berlyn MK, Blattner FR, Chaudhuri RR, Glasner JD, Horiuchi T, Keseler IM, Kosuge T, Mori H, Perna NT, Plunkett G, Rudd KE, Serres MH, Thomas GH, Thomson NR, Wishart D, Wanner BL (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34(1);1-9. PMID: 16397293

Serres01: Serres MH, Gopal S, Nahum LA, Liang P, Gaasterland T, Riley M (2001). "A functional update of the Escherichia coli K-12 genome." Genome Biol 2(9);RESEARCH0035. PMID: 11574054

Szumanski92: Szumanski MB, Boyle SM (1992). "Influence of cyclic AMP, agmatine, and a novel protein encoded by a flanking gene on speB (agmatine ureohydrolase) in Escherichia coli." J Bacteriol 174(3);758-64. PMID: 1310091

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt13: UniProt Consortium (2013). "UniProt version 2013-08 released on 2013-08-01 00:00:00." Database.

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

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

Other References Related to Gene Regulation

Kamenšek13: Kamenšek S, Žgur-Bertok D (2013). "Global transcriptional responses to the bacteriocin colicin M in Escherichia coli." BMC Microbiol 13;42. PMID: 23421615


Report Errors or Provide Feedback
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 Nov 27, 2014, BIOCYC13A.