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Escherichia coli K-12 substr. MG1655 Polypeptide: LolC



Gene: lolC Accession Numbers: G6573 (EcoCyc), b1116, ECK1102

Synonyms: ycfU

Regulation Summary Diagram: ?

Component of: LolCDE ABC lipoprotein transporter (extended summary available)

Summary:
LolC is the predicted membrane component of the LolCDE lipoprotein transporter [Yakushi00]. LolCDE is a unique member of the ATP-binding cassette (ABC) superfamily of transporters.

Locations: inner membrane

Map Position: [1,174,650 -> 1,175,849] (25.32 centisomes)
Length: 1200 bp / 399 aa

Molecular Weight of Polypeptide: 43.264 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0003772 , DIP:DIP-58651N , EchoBASE:EB3213 , EcoGene:EG13439 , EcoliWiki:b1116 , OU-Microarray:b1116 , PortEco:lolC , PR:PRO_000023105 , Pride:P0ADC3 , Protein Model Portal:P0ADC3 , RefSeq:NP_415634 , RegulonDB:G6573 , String:511145.b1116 , UniProt:P0ADC3

Relationship Links: InterPro:IN-FAMILY:IPR003838 , InterPro:IN-FAMILY:IPR011925 , InterPro:IN-FAMILY:IPR025857 , Pfam:IN-FAMILY:PF02687 , Pfam:IN-FAMILY:PF12704

In Paralogous Gene Group: 189 (15 members)

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0042953 - lipoprotein transport Inferred from experiment Inferred by computational analysis [GOA01a, Yakushi00]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
Molecular Function: GO:0042954 - lipoprotein transporter activity Inferred from experiment Inferred by computational analysis [GOA01a, Yakushi00]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Yakushi00]
GO:0043234 - protein complex Inferred from experiment [Yakushi00]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01a]

MultiFun Terms: cell structure membrane
transport Channel-type Transporters Pyrophosphate Bond (ATP; GTP; P2) Hydrolysis-driven Active Transporters The ATP-binding Cassette (ABC) Superfamily + ABC-type Uptake Permeases ABC superfamily, membrane component

Essentiality data for lolC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox No 37 Aerobic 7   No [Baba06, Comment 1]

Subunit of: LolCDE ABC lipoprotein transporter

Subunit composition of LolCDE ABC lipoprotein transporter = [LolE][LolD]2[LolC]

Summary:
Localization of lipoproteins to the periplasmic surface of the outer membrane in Escherichia coli requires a lipoprotein-specific sorting complex, made up of five proteins (LolABCDE) [Narita04].

Lipoproteins in E.coli, as well as in other bacteria, are membrane proteins that have covalently-attached lipids at their amino-terminal cysteine residue. Within the bacterial envelope of E. coli there are more than 90 species of lipoproteins, located on the periplasmic surfaces of both the inner and outer membrane, and responsible for a variety of functions. [Narita04].

All lipoproteins are thought to be synthesized with an N-terminal signal sequence which allows for their targeting to the Sec secretion system and subsequent translocation across the cytoplasmic membrane [Duong97]. After translocation across the cytoplasmic membrane, the signal peptide sequence is cleaved by lipoprotein-specific signal peptidase II followed by aminoacylation of the terminal cysteine residue [Pugsley93]. The mature form of the lipoprotein is then localized to either the inner or outer membrane. If the amino-acid residue next to the terminal cysteine is aspartate, then the lipoprotein is localized to the inner membrane. In all other cases, the lipoprotein is targeted for translocation across the periplasmic space to the outer membrane [Yamaguchi88].

LolA is a periplasmic proteinous factor which serves as a hydrophobic container, allowing for lipoproteins to become solubilized, thereby facilitating their translocation across the hydrophilic periplasmic space [Takeda03]. LolB is an outer membrane receptor for the LolA-lipoprotein complex [Yokota99]. LolCDE is a unique ABC transporter involved in the export of lipoproteins to the outer membrane [Yakushi00]. Sequence analysis indicates that LolC and LolE are integral membrane proteins and LolD is an ABC ATPase. In in vivo photo crosslinking studies LolA was observed to generate cross linked products with LolC but not with LolE suggesting that the two integral membrane components may have distinct functions [Okuda09]. LolCDE has been shown to be capable of utilizing ATP, GTP or UTP in the release process [Yakushi98], [Yakushi00].

Citations: [Narita06, Yasuda09]

Locations: inner membrane

GO Terms:

Biological Process: GO:0042953 - lipoprotein transport Inferred from experiment [Yakushi00]
Molecular Function: GO:0042954 - lipoprotein transporter activity Inferred from experiment [Yakushi00]
Cellular Component: GO:0005887 - integral component of plasma membrane Inferred by computational analysis Inferred from experiment [Yakushi00]
GO:0043234 - protein complex Inferred from experiment [Yakushi00]


Sequence Features

Feature Class Location Citations Comment
Transmembrane-Region 25 -> 45
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 270 -> 290
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 310 -> 330
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 358 -> 378
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

Daley05: Daley DO, Rapp M, Granseth E, Melen K, Drew D, von Heijne G (2005). "Global topology analysis of the Escherichia coli inner membrane proteome." Science 308(5726);1321-3. PMID: 15919996

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

Duong97: Duong F, Eichler J, Price A, Leonard MR, Wickner W (1997). "Biogenesis of the gram-negative bacterial envelope." Cell 91(5);567-73. PMID: 9393850

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

Narita04: Narita S, Matsuyama S, Tokuda H (2004). "Lipoprotein trafficking in Escherichia coli." Arch Microbiol 182(1);1-6. PMID: 15221203

Narita06: Narita S, Tokuda H (2006). "An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals." FEBS Lett 580(4);1164-70. PMID: 16288742

Okuda09: Okuda S, Tokuda H (2009). "Model of mouth-to-mouth transfer of bacterial lipoproteins through inner membrane LolC, periplasmic LolA, and outer membrane LolB." Proc Natl Acad Sci U S A 106(14);5877-82. PMID: 19307584

Pugsley93: Pugsley AP (1993). "The complete general secretory pathway in gram-negative bacteria." Microbiol Rev 57(1);50-108. PMID: 8096622

Takeda03: Takeda K, Miyatake H, Yokota N, Matsuyama S, Tokuda H, Miki K (2003). "Crystal structures of bacterial lipoprotein localization factors, LolA and LolB." EMBO J 22(13);3199-209. PMID: 12839983

UniProt10: 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."

Yakushi00: Yakushi T, Masuda K, Narita S, Matsuyama S, Tokuda H (2000). "A new ABC transporter mediating the detachment of lipid-modified proteins from membranes." Nat Cell Biol 2(4);212-8. PMID: 10783239

Yakushi98: Yakushi T, Yokota N, Matsuyama S, Tokuda H (1998). "LolA-dependent release of a lipid-modified protein from the inner membrane of Escherichia coli requires nucleoside triphosphate." J Biol Chem 273(49);32576-81. PMID: 9829994

Yamaguchi88: Yamaguchi K, Yu F, Inouye M (1988). "A single amino acid determinant of the membrane localization of lipoproteins in E. coli." Cell 53(3);423-32. PMID: 3284654

Yasuda09: Yasuda M, Iguchi-Yokoyama A, Matsuyama S, Tokuda H, Narita S (2009). "Membrane topology and functional importance of the periplasmic region of ABC transporter LolCDE." Biosci Biotechnol Biochem 73(10);2310-6. PMID: 19809197

Yokota99: Yokota N, Kuroda T, Matsuyama S, Tokuda H (1999). "Characterization of the LolA-LolB system as the general lipoprotein localization mechanism of Escherichia coli." J Biol Chem 274(43);30995-9. PMID: 10521496

Zhang07: Zhang N, Chen R, Young N, Wishart D, Winter P, Weiner JH, Li L (2007). "Comparison of SDS- and methanol-assisted protein solubilization and digestion methods for Escherichia coli membrane proteome analysis by 2-D LC-MS/MS." Proteomics 7(4);484-93. PMID: 17309111


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 Sat Dec 20, 2014, biocyc12.