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Escherichia coli K-12 substr. MG1655 Polypeptide: flagellar hook protein FlgE



Gene: flgE Accession Numbers: G361 (EcoCyc), b1076, ECK1061

Synonyms: flaFV, flaK

Regulation Summary Diagram: ?

Component of: Flagellum (extended summary available)

Summary:
FlgE is the basic subunit that polymerizes to form the flexible hook structure which couples the envelope-embedded flagellar rotary motor to the rigid flagellar filament in Escherichia coli.

Gene Citations: [Jones87b, Macnab92, Fahrner94]

Locations: cytosol, cell projection

Map Position: [1,131,797 -> 1,133,005] (24.39 centisomes)
Length: 1209 bp / 402 aa

Molecular Weight of Polypeptide: 42.045 kD (from nucleotide sequence), 42 kD (experimental) [Komeda78 ]

Unification Links: ASAP:ABE-0003647 , CGSC:766 , EchoBASE:EB4017 , EcoGene:EG14269 , EcoliWiki:b1076 , OU-Microarray:b1076 , PortEco:flgE , PR:PRO_000022641 , Pride:P75937 , Protein Model Portal:P75937 , RefSeq:NP_415594 , RegulonDB:G361 , SMR:P75937 , String:511145.b1076 , Swiss-Model:P75937 , UniProt:P75937

Relationship Links: InterPro:IN-FAMILY:IPR001444 , InterPro:IN-FAMILY:IPR010930 , InterPro:IN-FAMILY:IPR011491 , InterPro:IN-FAMILY:IPR019776 , InterPro:IN-FAMILY:IPR020013 , Pfam:IN-FAMILY:PF00460 , Pfam:IN-FAMILY:PF06429 , Pfam:IN-FAMILY:PF07559 , Prosite:IN-FAMILY:PS00588

In Paralogous Gene Group: 250 (3 members)

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment [LopezCampistrou05]
GO:0009424 - bacterial-type flagellum hook Inferred from experiment [Komeda84, Komeda78a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11a]
GO:0030694 - bacterial-type flagellum basal body, rod Inferred by computational analysis [GOA01]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum

Essentiality data for flgE 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 ? 31-Oct-2006 by Johnson A , TIGR


Subunit of: Flagellum

Subunit composition of Flagellum = [([FliG]26[FliM]34[FliN])(FlgH)(MotA)(MotB)(FlgB)(FlgC)(FlgF)(FlgG)(FlgI)(FliF)(FliE)][(FlhA)(FlhB)(FliO)(FliP)(FliQ)(FliR)(FliH)12(FliI)6(FliJ)][FlgE]120[FlgK][FlgL][FliC][FliD]5
         Flagellar Motor Complex = ([FliG]26[FliM]34[FliN])(FlgH)(MotA)(MotB)(FlgB)(FlgC)(FlgF)(FlgG)(FlgI)(FliF)(FliE) (extended summary available)
                 Flagellar Motor Switch Complex = (FliG)26(FliM)34(FliN) (extended summary available)
                         flagellar motor switch protein FliG = FliG (summary available)
                         flagellar motor switch protein FliM = FliM (summary available)
                         flagellar motor switch protein FliN = FliN (summary available)
                 flagellar L-ring protein FlgH; basal-body outer-membrane L (lipopolysaccharide layer) ring protein = FlgH (summary available)
                 MotA protein, proton conductor component of motor; no effect on switching = MotA (summary available)
                 MotB protein, enables flagellar motor rotation, linking torque machinery to cell wall = MotB (summary available)
                 flagellar basal-body rod protein FlgB = FlgB (summary available)
                 flagellar basal-body rod protein FlgC = FlgC (summary available)
                 flagellar basal-body rod protein FlgF = FlgF (summary available)
                 flagellar basal-body rod protein FlgG = FlgG (summary available)
                 flagellar P-ring protein FlgI = FlgI (summary available)
                 flagellar M-ring protein FliF; basal-body MS(membrane and supramembrane)-ring and collar protein = FliF (summary available)
                 flagellar basal-body protein FliE = FliE (summary available)
         Flagellar Export Apparatus = (FlhA)(FlhB)(FliO)(FliP)(FliQ)(FliR)(FliH)12(FliI)6(FliJ) (extended summary available)
                 flagellar biosynthesis protein FlhA = FlhA (summary available)
                 flagellar biosynthesis protein FlhB = FlhB (summary available)
                 flagellar biosynthesis protein FliO = FliO (summary available)
                 flagellar biosynthesis protein FliP = FliP (summary available)
                 flagellar biosynthesis protein FliQ = FliQ (summary available)
                 flagellar biosynthesis protein FliR = FliR (summary available)
                 flagellar biosynthesis protein FliH = FliH (summary available)
                 flagellum-specific ATP synthase FliI = FliI (summary available)
                 flagellar biosynthesis protein FliJ = FliJ (summary available)
         flagellar hook protein FlgE = FlgE (summary available)
         flagellar biosynthesis, hook-filament junction protein 1 = FlgK (summary available)
         flagellar biosynthesis; hook-filament junction protein = FlgL (summary available)
         flagellar biosynthesis; flagellin, filament structural protein = FliC (summary available)
         flagellar cap protein FliD; filament capping protein; enables filament assembly = FliD (summary available)

Summary:
The flagellum is a molecular machine with a proton motive force driven rotary motor which rotates a long, curved filament allowing the cell to swim in a liquid environment. Some of the evidence for the structure and function of the flagellum comes from experiments involving Salmonella typhiumurium flagella; however, this evidence is generally believed to apply to the homologous system in E. coli as well.

The three major components of the flagellum are the basal body located within the membranes, and the hook and filament which extend from the basal body outward. The basal body contains the Flagellar Motor Complex and the Flagellar Export Apparatus. The hook is a polymer of FlgE proteins connected to the rod of the basal body. The filament is a polymer of FliC proteins joined to the hook by the FlgK and FlgL hook-filament junction proteins and capped by the filament capping protein, FliD.

The FlgE subunits form 11 parallel rows or protofilaments on the hook's cylindrical surface. Two hook filament junction proteins, FlgK and FlgL, join the hook to the filament [Berg03]. FlgK and FlgL are exported from the cytoplasm with the help of the chaperone FlgN [Fraser99b, Bennett01] via the type III flagellar export apparatus once hook assembly is complete [Kutsukake94].

The 20,000 or so FliC subunits form 11 parallel rows or protofilaments on the filament's cylindrical surface. There are two packing configurations which result in either a left- or a right-handed helical orientation depending on whether the subunits are packed into "long" or "short" protofilaments, respectively. If both types of protofilaments are present simultaneously, the helical filament has both curvature as well as twist with the short protofilaments aligned along the inside of the helix. Each filament is driven at a rotational speed of around 100 Hz by a membrane-embedded rotary motor at its base capable of switching direction of rotation in response to signals from the chemotaxis system. Flagellar/motor complexes are located peritrichously around the outside of the cell with 4, on average, per cell. They originate at random points on its sides and extend several cell body lengths out into the medium. During smooth swimming, their rotation is counterclockwise, causing the flagella to bundle together and propel the cell forward. When the flagellar motor switches to clockwise, the filament's helical orientation transforms from a left-handed supercoil to a right-handed supercoil. The transformation first occurs at the base of the filaments and propagates quickly to the distal end causing the filament bundles to fall apart smoothly which results in tumbling. The run usually lasts for a few seconds followed by the tumble for a fraction of a second. The flagellar filament is connected proximally to a flexible hook structure which is a polymer of FlgE subunits, via two hook-filament junction proteins (FlgK and FlgL) and distally to the flagellar cap, FliD [Hasegawa98, Berg03, Samatey01].

The cap complex consists of five subunits of FliD, which form a pentagonal plate domain and axially extended leg-like domains which insert into cavities at the distal end of the growing filament [Maki98]. The resulting space formed under the cap plate serves as a folding chamber for the FliC flagellin subunits that have just been exported to the distal end of the nascent flagella [Yonekura00]. The leg-like domains of the flagellar cap allow for limited flexibility, permitting insertion of newly folded FliC into an indentation or open gap caused by a symmetry mismatch between the cap and the filament's distal end [Yonekura00]. Upon incorporation of a FliC monomer into the indentation, the cap complex rotates and moves up through conformational rearrangement of the leg-like domains. This creates a new open gap indentation which serves as the next flagellin binding site [MakiYonekura03, Minamino04].

Credits:
Created 31-Oct-2006 by Johnson A , TIGR


Sequence Features

Feature Class Location Citations Comment
Cleavage-of-Initial-Methionine 1
[UniProt10a]
UniProt: Removed; Non-Experimental Qualifier: by similarity;
Chain 2 -> 402
[UniProt09]
UniProt: Flagellar hook protein flgE;


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1076 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene G361.


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

Bennett01: Bennett JC, Thomas J, Fraser GM, Hughes C (2001). "Substrate complexes and domain organization of the Salmonella flagellar export chaperones FlgN and FliT." Mol Microbiol 39(3);781-91. PMID: 11169117

Berg03: Berg HC (2003). "The rotary motor of bacterial flagella." Annu Rev Biochem 72;19-54. PMID: 12500982

Fahrner94: Fahrner KA, Block SM, Krishnaswamy S, Parkinson JS, Berg HC (1994). "A mutant hook-associated protein (HAP3) facilitates torsionally induced transformations of the flagellar filament of Escherichia coli." J Mol Biol 1994;238(2);173-86. PMID: 8158647

Fraser99b: Fraser GM, Bennett JC, Hughes C (1999). "Substrate-specific binding of hook-associated proteins by FlgN and FliT, putative chaperones for flagellum assembly." Mol Microbiol 32(3);569-80. PMID: 10320579

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."

Hasegawa98: Hasegawa K, Yamashita I, Namba K (1998). "Quasi- and nonequivalence in the structure of bacterial flagellar filament." Biophys J 74(1);569-75. PMID: 9449357

Jones87b: Jones CJ, Homma M, Macnab RM (1987). "Identification of proteins of the outer (L and P) rings of the flagellar basal body of Escherichia coli." J Bacteriol 1987;169(4);1489-92. PMID: 3549690

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

Komeda78: Komeda Y, Silverman M, Matsumura P, Simon M (1978). "Genes for the hook-basal body proteins of the flagellar apparatus in Escherichia coli." J Bacteriol 134(2);655-67. PMID: 350831

Komeda78a: Komeda Y, Silverman M, Simon M (1978). "Identification of the structural gene for the hook subunit protein of Escherichia coli flagella." J Bacteriol 133(1);364-71. PMID: 338588

Komeda84: Komeda Y, Ono N, Kagawa H (1984). "Synthesis of flagellin and hook subunit protein in flagellar mutants of Escherichia coli K12." Mol Gen Genet 194(1-2);49-51. PMID: 6374380

Kutsukake94: Kutsukake K, Minamino T, Yokoseki T (1994). "Isolation and characterization of FliK-independent flagellation mutants from Salmonella typhimurium." J Bacteriol 176(24);7625-9. PMID: 8002586

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

Macnab92: Macnab RM (1992). "Genetics and biogenesis of bacterial flagella." Annu Rev Genet 1992;26;131-58. PMID: 1482109

Maki98: Maki S, Vonderviszt F, Furukawa Y, Imada K, Namba K (1998). "Plugging interactions of HAP2 pentamer into the distal end of flagellar filament revealed by electron microscopy." J Mol Biol 277(4);771-7. PMID: 9545371

MakiYonekura03: Maki-Yonekura S, Yonekura K, Namba K (2003). "Domain movements of HAP2 in the cap-filament complex formation and growth process of the bacterial flagellum." Proc Natl Acad Sci U S A 100(26);15528-33. PMID: 14673116

Minamino04: Minamino T, Namba K (2004). "Self-assembly and type III protein export of the bacterial flagellum." J Mol Microbiol Biotechnol 7(1-2);5-17. PMID: 15170399

Samatey01: Samatey FA, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, Yamamoto M, Namba K (2001). "Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling." Nature 410(6826);331-7. PMID: 11268201

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

Yonekura00: Yonekura K, Maki S, Morgan DG, DeRosier DJ, Vonderviszt F, Imada K, Namba K (2000). "The bacterial flagellar cap as the rotary promoter of flagellin self-assembly." Science 290(5499);2148-52. PMID: 11118149

Other References Related to Gene Regulation

Stafford05: Stafford GP, Ogi T, Hughes C (2005). "Binding and transcriptional activation of non-flagellar genes by the Escherichia coli flagellar master regulator FlhD2C2." Microbiology 151(Pt 6);1779-88. PMID: 15941987

Theodorou12: Theodorou MC, Theodorou EC, Kyriakidis DA (2012). "Involvement of AtoSC two-component system in Escherichia coli flagellar regulon." Amino Acids 43(2);833-44. PMID: 22083893


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 Sun Nov 23, 2014, BIOCYC13B.