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Escherichia coli K-12 substr. MG1655 Polypeptide: flagellar biosynthesis protein FlhB



Gene: flhB Accession Numbers: G7028 (EcoCyc), b1880, ECK1881

Synonyms: yecQ, flaG

Regulation Summary Diagram: ?

Component of:
Flagellar Export Apparatus (extended summary available)
Flagellum (extended summary available)

Summary:
FlhB is one of six integral membrane components of the flagellar export apparatus. FlhB has two regions: the hydrophobic N-terminal domain which, according to hydophobicity studies, crosses the cytoplasmic membrane four times and the C-terminal cytoplasmic domain [Kutsukake94].

Locations: inner membrane

Map Position: [1,963,067 <- 1,964,215] (42.31 centisomes)
Length: 1149 bp / 382 aa

Molecular Weight of Polypeptide: 42.238 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006275 , EchoBASE:EB3789 , EcoGene:EG14035 , EcoliWiki:b1880 , OU-Microarray:b1880 , PortEco:flhB , PR:PRO_000022651 , Pride:P76299 , Protein Model Portal:P76299 , RefSeq:NP_416394 , RegulonDB:G7028 , SMR:P76299 , String:511145.b1880 , UniProt:P76299

Relationship Links: InterPro:IN-FAMILY:IPR006135 , InterPro:IN-FAMILY:IPR006136 , Pfam:IN-FAMILY:PF01312 , Prints:IN-FAMILY:PR00950

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01a]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11, GOA01a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11, GOA01a]

MultiFun Terms: cell structure flagella
cell structure membrane

Essentiality data for flhB 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]

Subunit of: Flagellar Export Apparatus

Subunit composition of Flagellar Export Apparatus = [FlhA][FlhB][FliO][FliP][FliQ][FliR][FliH]12[FliI]6[FliJ]
         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)

Component of: Flagellum (extended summary available)

Summary:
The flagellar export apparatus is a type III secretion system that functions in the export of several components of the flagellum across the cytoplasmic membrane into the channel of the flagellum for assembly. The export apparatus consists of six integral membrane proteins (FliO, FliP, FliQ, FliR, FlhA, and FlhB) and three soluble proteins (FliH, FliI, and FliJ) and interacts with several soluble chaperones (FliS, FliT, and FlgN) and the hook-length control protein (FliK). The flagellar motor switch complex proteins (FliG, FliM, and FliN) also take part in interactions affecting protein export.

The six integral membrane proteins of the flagellar export apparatus are embedded in the membrane within the MS ring of the basal body where the apparatus can deliver substrates across the cytoplasmic membrane to the distal end of the growing flagellum [Minamino04]. It is thought that FliO, FliP, FliQ, FliR, FlhA and FlhB comprise the protein-conducting channel of the flagellar export apparatus [Minamino99]. Binding studies show that the FlhA cytoplasmic region associates with FliH, FliI and FliJ as well as with the cytoplasmic domain of FlhB and flagellar export substrates, and that the cytoplasmic region of FlhB associates with FliH, FliI, and FliJ [Minamino00, Zhu02]. The transmembrane region of FlhA interacts with the MS ring [Kihara01]. FlhA has also been shown to interact with FliO, FliP, and FliQ [McMurry04].

FliI is a cytoplasmic component of the export apparatus and serves as the ATPase, providing the energy for translocation of export substrates across the cytoplasmic membrane [Fan96]. FliI exists as a monomer in solution [Minamino00a] but is capable of forming a heterotrimeric complex with a dimer of the cytoplasmic protein FliH, the FliI inhibitor. FliH inhibits FliI ATPase activity to conserve energy until protein export can occur by preventing premature oligomerization of FliI [Minamino06]. FliH also acts in targeting of FliI to the export apparatus by binding the FliN protein of the motor switch complex [McMurry06]. In its active form, in the presence of ATP, FliI undergoes oligomerization, forming a hexameric ring structure that binding studies have indicated associates with the cytoplasmic domains of FlhB and FlhA [Minamino00, Zhu02]. The ATPase activity of FliI has been shown to be cooperative, suggesting that the oligomerization of FliI plays a physiologically significant role [Claret03]. It is unclear whether FliH dissociates from the complex when FliI attaches to the export apparatus [Minamino06]. Binding studies also indicate FliH interacts with FlhA and FlhB [Minamino00, Zhu02], as well as FliJ [GonzalezPedrajo02]. FliH is not essential for flagellar protein export [Minamino03]. FliJ has been shown to suppress self-aggregation of several flagellar export substrates [Minamino00b]. Mutation studies showed that FliJ is a general component of the flagellar export apparatus that displays chaperone-like activity for both rod/hook-type and filament-type export substrates [Minamino00c]. Binding studies indicate FliJ interacts with both FliH and FlhA [GonzalezPedrajo02, Fraser03], as well as FliM, though the presence of FliJ weakens FliM/FliN and FliN/FliH interactions [GonzalezPedrajo06].

The proteins of the flagellar motor switch complex are also involved in flagellar assembly because null mutations are non-flagellate. FliN is responsible for binding of substrate-bound cytosolic components of the flagellar export apparatus to direct them to the membrane components for export of the substrate. Co-purification studies reveal complexes of FliG, FliM, FliN, FliH, and FliI [GonzalezPedrajo06]. FliN was shown to bind FliH in a manner that does not disrupt the FliM/FliN and FliH/FliI interactions.

In order to make assembly of the flagellum more efficient, proteins required early in the assembly process, such as hook and rod proteins, are transported before proteins of more distal structures. There are two main specificity classes of exported proteins: the rod/hook type and the filament type. The initial state of the export apparatus involves export of rod/hook type substrates, which include FliE, FlgB, FlgC, FlgD, FlgE, FlgF, FlgG, FlgJ, and FliK. FlhB, along with hook-length control protein FliK, coordinates the switching in export specificity from rod/hook-type proteins to filament-type proteins [Kubori00]. FliK is the sensor and transmitter of the hook completion signal [Minamino04a]. An "infrequent ruler function model" suggest the N-terminal domain of FliK, which binds both FlgE and FlgD proteins, acts as a molecular ruler to determine when the hook has reached the appropriate length [Moriya06, Minamino06a]. The model also suggests that the timing of the hook completion signal is determined when a FliK protein happens to be transported at a time when the hook is of approximately the correct length [Moriya06, Minamino06a]. This is supported by the fact that FliK has no apparent function within the periplasm [Hirano05]. Upon completion of the flagellar hook structure, the C-terminal domain of FliK is able to communicate directly with the C-terminal cytoplasmic domain FlhB [Minamino00b, Minamino04a], which undergoes autocatalytic cleavage producing FlhB(CN) and FlhB(CC), which remain tightly associated [Ferris05]. This results in switching of export substrate specificity from rod/hook-type proteins to filament-type proteins, which include FlgK, FlgL, FlgM, FliC, and FliD [Minamino04].

FlgN acts as a chaperone for FlgK and FlgL. FliS and FliT act as a chaperones for FliC and FliD, respectively. Mutation studies show that the FlgNK, FlgNL, FliSC, and FliTD substrate-chaperone complexes dock at FliI for export of the substrates [Thomas04].

Credits:
Created 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
Transmembrane-Region 32 -> 52
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 74 -> 94
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 95 -> 115
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 145 -> 165
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Transmembrane-Region 190 -> 210
[UniProt10]
UniProt: Helical;; Non-Experimental Qualifier: potential;
Sequence-Conflict 250
[Cho97, UniProt10a]
Alternate sequence: A → R; UniProt: (in Ref. 1; AAC17834);
Sequence-Conflict 316
[Cho97, UniProt10a]
Alternate sequence: P → R; UniProt: (in Ref. 1; AAC17834);


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
3/2/1998 (pkarp) Merged genes G371/flhB and G7028/flhB
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

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

Cho97: Cho M., Matsumura P. (1997). "Genomic organization of flhB operon in E.coli." Data submission to EMBL/GenBank/DDBJ databases on 1997-02.

Claret03: Claret L, Calder SR, Higgins M, Hughes C (2003). "Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly." Mol Microbiol 48(5);1349-55. PMID: 12787361

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

Fan96: Fan F, Macnab RM (1996). "Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium." J Biol Chem 271(50);31981-8. PMID: 8943245

Ferris05: Ferris HU, Furukawa Y, Minamino T, Kroetz MB, Kihara M, Namba K, Macnab RM (2005). "FlhB regulates ordered export of flagellar components via autocleavage mechanism." J Biol Chem 280(50);41236-42. PMID: 16246842

Fraser03: Fraser GM, Gonzalez-Pedrajo B, Tame JR, Macnab RM (2003). "Interactions of FliJ with the Salmonella type III flagellar export apparatus." J Bacteriol 185(18);5546-54. PMID: 12949107

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

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

GonzalezPedrajo02: Gonzalez-Pedrajo B, Fraser GM, Minamino T, Macnab RM (2002). "Molecular dissection of Salmonella FliH, a regulator of the ATPase FliI and the type III flagellar protein export pathway." Mol Microbiol 45(4);967-82. PMID: 12180917

GonzalezPedrajo06: Gonzalez-Pedrajo B, Minamino T, Kihara M, Namba K (2006). "Interactions between C ring proteins and export apparatus components: a possible mechanism for facilitating type III protein export." Mol Microbiol 60(4);984-98. PMID: 16677309

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

Hirano05: Hirano T, Shibata S, Ohnishi K, Tani T, Aizawa S (2005). "N-terminal signal region of FliK is dispensable for length control of the flagellar hook." Mol Microbiol 56(2);346-60. PMID: 15813729

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

Kihara01: Kihara M, Minamino T, Yamaguchi S, Macnab RM (2001). "Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus." J Bacteriol 183(5);1655-62. PMID: 11160096

Kubori00: Kubori T, Sukhan A, Aizawa SI, Galan JE (2000). "Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system." Proc Natl Acad Sci U S A 97(18);10225-30. PMID: 10944190

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

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

McMurry04: McMurry JL, Van Arnam JS, Kihara M, Macnab RM (2004). "Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machinery." J Bacteriol 186(22);7586-92. PMID: 15516571

McMurry06: McMurry JL, Murphy JW, Gonzalez-Pedrajo B (2006). "The FliN-FliH interaction mediates localization of flagellar export ATPase FliI to the C ring complex." Biochemistry 45(39);11790-8. PMID: 17002279

Minamino00: Minamino T, MacNab RM (2000). "Interactions among components of the Salmonella flagellar export apparatus and its substrates." Mol Microbiol 35(5);1052-64. PMID: 10712687

Minamino00a: Minamino T, MacNab RM (2000). "FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity." Mol Microbiol 37(6);1494-503. PMID: 10998179

Minamino00b: Minamino T, Macnab RM (2000). "Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switching." J Bacteriol 182(17);4906-14. PMID: 10940035

Minamino00c: Minamino T, Chu R, Yamaguchi S, Macnab RM (2000). "Role of FliJ in flagellar protein export in Salmonella." J Bacteriol 182(15);4207-15. PMID: 10894728

Minamino03: Minamino T, Gonzalez-Pedrajo B, Kihara M, Namba K, Macnab RM (2003). "The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH." J Bacteriol 185(13);3983-8. PMID: 12813095

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

Minamino04a: Minamino T, Saijo-Hamano Y, Furukawa Y, Gonzalez-Pedrajo B, Macnab RM, Namba K (2004). "Domain organization and function of Salmonella FliK, a flagellar hook-length control protein." J Mol Biol 341(2);491-502. PMID: 15276839

Minamino06: Minamino T, Kazetani K, Tahara A, Suzuki H, Furukawa Y, Kihara M, Namba K (2006). "Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region." J Mol Biol 360(2);510-9. PMID: 16780875

Minamino06a: Minamino T, Ferris HU, Moriya N, Kihara M, Namba K (2006). "Two parts of the T3S4 domain of the hook-length control protein FliK are essential for the substrate specificity switching of the flagellar type III export apparatus." J Mol Biol 362(5);1148-58. PMID: 16949608

Minamino99: Minamino T, Macnab RM (1999). "Components of the Salmonella flagellar export apparatus and classification of export substrates." J Bacteriol 181(5);1388-94. PMID: 10049367

Moriya06: Moriya N, Minamino T, Hughes KT, Macnab RM, Namba K (2006). "The type III flagellar export specificity switch is dependent on FliK ruler and a molecular clock." J Mol Biol 359(2);466-77. PMID: 16630628

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

Thomas04: Thomas J, Stafford GP, Hughes C (2004). "Docking of cytosolic chaperone-substrate complexes at the membrane ATPase during flagellar type III protein export." Proc Natl Acad Sci U S A 101(11);3945-50. PMID: 15001708

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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

Zhu02: Zhu K, Gonzalez-Pedrajo B, Macnab RM (2002). "Interactions among membrane and soluble components of the flagellar export apparatus of Salmonella." Biochemistry 41(30);9516-24. PMID: 12135374

Other References Related to Gene Regulation

Liu94: Liu X, Matsumura P (1994). "The FlhD/FlhC complex, a transcriptional activator of the Escherichia coli flagellar class II operons." J Bacteriol 176(23);7345-51. PMID: 7961507

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


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, BIOCYC14A.