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Escherichia coli K-12 substr. MG1655 Polypeptide: MotB protein, enables flagellar motor rotation, linking torque machinery to cell wall



Gene: motB Accession Numbers: EG10602 (EcoCyc), b1889, ECK1890

Synonyms: flaJ

Regulation Summary Diagram: ?

Component of:
Flagellar Motor Complex (extended summary available)
Flagellum (extended summary available)

Summary:
MotB and MotA comprise the stator element of the flagellar motor complex.

Gene Citations: [Silverman77, Mirel92]

Locations: inner membrane

Map Position: [1,973,353 <- 1,974,279] (42.53 centisomes)
Length: 927 bp / 308 aa

Molecular Weight of Polypeptide: 34.186 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0006297 , CGSC:490 , DIP:DIP-47996N , EchoBASE:EB0597 , EcoGene:EG10602 , EcoliWiki:b1889 , ModBase:P0AF06 , OU-Microarray:b1889 , PortEco:motB , PR:PRO_000023275 , Pride:P0AF06 , Protein Model Portal:P0AF06 , RefSeq:NP_416403 , RegulonDB:EG10602 , SMR:P0AF06 , String:511145.b1889 , UniProt:P0AF06

Relationship Links: InterPro:IN-FAMILY:IPR006665 , InterPro:IN-FAMILY:IPR025713 , Pfam:IN-FAMILY:PF00691 , Pfam:IN-FAMILY:PF13677 , Prosite:IN-FAMILY:PS51123

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11a, UniProtGOA11, Wilson90]
GO:0016021 - integral component of membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, Wilson90]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11]

MultiFun Terms: cell processes motility, chemotaxis, energytaxis (aerotaxis, redoxtaxis etc)
cell structure flagella
cell structure membrane
transport Channel-type Transporters alpha-type channels

Essentiality data for motB 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: Flagellar Motor Complex

Subunit composition of Flagellar Motor Complex = [(FliG)26(FliM)34(FliN)][FlgH][MotA][MotB][FlgB][FlgC][FlgF][FlgG][FlgI][FliF][FliE]
         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)

Component of: Flagellum (extended summary available)

Summary:
The bacterial flagellar motor of Escherichia coli is a complex of about 20 different parts no more than 50 nm in diameter. It is capable of spinning clockwise (CW) or counterclockwise (CCW) at speeds approaching 100 Hz, propelling the corkscrew shaped flagellar filaments (FliC subunits) and generating motion. E. coli are peritrichously flagellated (peri, around, trichos, hair) with usually four motor/filament structures arranged randomly around the sides of the cell and extending out several body lengths. When the motors turn CCW, the filaments bundle together in a coordinated effort which pushes the cell steadily forward in a "run". Conversely, when the direction of motor rotation is switched to CW, the coordination of the flagellar bundle is disrupted and the cell tumbles randomly and then starts out in a new direction based on concentrations of attractants or repellents which control the motor switching mechanism [Berg03]. Flagella motors also adapt to mechanical stimuli (ie. sudden changes in load) by changing their speed and CW bias [Lele13].

The bacterial flagellar motor core is made up of a complex group of protein constituents. There are four rod proteins (FlgB, FlgC, FlgF and FlgG) and three ring proteins (FlgH, FlgI and FliF) which form the L, P and MS rings, respectively. These three rings, through which the rod passes, are embedded in the cell wall. The outer two rings, L (FlgH) and P (FlgI), are spaced apart and linked by a cylindrical wall. The inner two rings, S and M, are in direct contact and comprise a single protein (FliF) known as the "MS ring". The three rings, according to their known biochemical and geometrical properties, occupy distinct locations within the intact cell, with the L ring in the plane of the outer lipopolysaccharide membrane, the P ring in the plane of the peptidoglycan layer and the MS ring (membrane/supramembrane) in and above the cell membrane [Berg03].

The MS ring is the first substructure of the flagellar structure to be assembled and serves as the base structure for bacterial flagellar assembly and to anchor the flagellum in the cytoplasmic membrane [Grunenfelder03, Suzuki98]. There are about 26 copies of FliF monomer in each MS (membrane and supramembrane) ring complex [Sosinsky92]. The complex consists of the MS rings as well as a proximal portion of the rod in the flagellar basal body [Suzuki98]. FliF is firmly attached to the distal side of FliG, which interacts with the stator protein complex to generate torque [Suzuki04]. Assembly of the MS ring can occur in the absence of any of the other components of the flagellar structure [Katayama96] and the subsequent distal structural components (with the exception of the P and the L rings) are assembled via single-file export through the MS ring structure coupled with the transport apparatus complex of proteins [Macnab03]. This type of export is termed the flagellar-specific type III secretion system and it is highly similar in appearance and sequence homology to the type III pathways used for virulence secretion. The P and L rings are exported through the primary, or Sec, pathway [Macnab03].

FliE is a component of the basal body assembly. FliE has been shown to physically interact with FlgB and is thought to be a structural adapter between the FliF (MS) ring and the rod, a rotational component which is situated transverse to the outer membrane and peptidoglycan layers [Minamino00].

FlgB, FlgC, FlgF, and FlgG are four proteins that comprise the rod section of the basal-body assembly of the flagellar motor. The rod is a rotational component which is situated transverse to the outer membrane and peptidoglycan layers and is circumscribed by a set of four rings which lie in a horizontal plane within the inner and outer membranes of the cell envelope. The rod acts as a drive shaft to transmit torque from the motor through the flexible hook to the flagellar filament thus allowing for bacterial locomotion [Jones90]. FlgG is a distal component of the basal body rod [SaijoHamano04, Berg03].

FliM and FliN make up the C-ring, which is located inside (cytoplasmic) the cell. Together with FliG, FliM and FliN make up the switch complex which is essential for assembly, rotation and directional control [Welch93]. Although at least one study [Thomas99] suggests that the MS and C rings rotate relative to one another, the consensus seems to be that the MS and the C-rings rotate as a unit, and together form the rotor of the motor. Mutation deletion studies of the fliG, fliM and fliN [Yamaguchi86] resulted in defects in motor rotation control.

MotA and MotB are thought to form a torque-generating stator complex. MotA and MotB have shown to co-isolate in binding studies [Tang96]. MotA and MotB are membrane embedded and do not fractionate with the other hook-basal body proteins [Ridgway77]. Both proteins span the cytoplasmic membrane with MotA having four membrane-spanning alpha-helical segments and about two-thirds of its mass in the cytoplasm [Blair91, Zhou95a]. MotB has one membrane-spanning alpha-helix but the majority of the molecule is in the periplasmic space with a peptidoglycan-binding domain near its C-terminus [Chun88]. MotB is thought to anchor MotA to the cell wall's rigid framework, allowing the MotA/MotB complex to serve as the stationary stator of the flagellar motor [Berg03]. Mutations in MotB near the region where it is thought to be bound to the peptidoglycan region result in the apparent misalignment of the stator and rotor [Garza96]. MotA and MotB are arranged in a circular fashion around the MS and C-rings. In freeze-fracture electron microscopy, MotA and MotB can be visualized as circular "ring particles" or "studs" lying in a plane within the inner membrane of Escherichia coli [Khan88]. The stoichiometric composition per motor has been determined as being MotA4 MotB2 [Kojima04, Braun04]. Studies using GFP-labeled MotB revealed 11 stators per motor complex, each composed of two copies of MotB and four copies of MotA [Reid06, Leake06]. Direct observation of rotation steps in a Na+-driven chimaeric flagellar motor supports the evidence for 11 stators per motor complex [Sowa05]. The results from cross-linking studies have been used to examine the organization of some transmembrane helices in MotA and MotB and to develop a model for the overall organization of the entire MotA-MotB complex [Kim08].

The MotA/MotB complex conducts protons across the membrane and then couples this proton flow to rotational torque of the motor [Kojima04] in a process that involves the protonation/deprotonation of the Asp32 residue of MotB [Zhou98b, Braun01]. Two proton channels are formed per complex, with two copies of MotA forming eight transmembrane segments and one additional transmembrane segment coming from one copy of MotB [Braun04]. Mutation suppression studies of motA and motB [Garza96a, Garza95] indicate that MotA and MotB may interact with each other as well as with FliG (which is located at the cytoplasmic face at the periphery of the MS-ring and is thought to comprise part of the rotor of the flagellar motor). Charged residues have been defined in MotA's cytoplasmic domain which are critical for interaction with oppositely charged groups in the C-terminal domain of FliG [Zhou97, Zhou98c, Yakushi06]. The electrostatic interactions between these pairs of charged groups at the rotor-stator interface are thought to play a significant role in torque generation. The torque necessary for flagellar rotation, then, is apparently generated by the protonation and deprotonation of Asp32 of MotB, which then results in a conformational modulation of MotA. This results in an alteration in the interactions between a specific charged region of MotA's cytoplasmic domain and a complementary charged region in the C-terminal domain of FliG [Berg03].

Deletion mutation studies [Macnab92] have shown that FliG, FliM, FliN, MotA and MotB are the only proteins that function specifically in motor rotation since mutations in only these proteins result in cessation of rotation but not in flagellar assembly.

Reviews: [Morimoto14]


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 [Fraser99, 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 28 -> 49
[UniProt10a]
UniProt: Helical; Signal-anchor for type II membrane protein;; Non-Experimental Qualifier: probable;
Mutagenesis-Variant 31
[UniProt10]
Alternate sequence: A → T; UniProt: Complete loss of motility;
Mutagenesis-Variant 32
[Blair91a, UniProt11]
Alternate sequence: D → N; UniProt: Complete loss of motility.
Mutagenesis-Variant 39
[Blair91a, UniProt11]
Alternate sequence: A → V; UniProt: Complete loss of motility.
Acetylation-Modification 107
[Yu08]
 
Conserved-Region 148 -> 268
[UniProt09]
UniProt: OmpA-like;
Mutagenesis-Variant 159
[Blair91a, UniProt11]
Alternate sequence: P → I; UniProt: Decreased motility, subnormal torque, tethered strains rotate very slowly.
Mutagenesis-Variant 164
[Blair91a, UniProt11]
Alternate sequence: G → D; UniProt: Complete loss of motility.
Mutagenesis-Variant 196
[Blair91a, UniProt11]
Alternate sequence: T → I; UniProt: Complete loss of motility.
Mutagenesis-Variant 197
[Blair91a, UniProt11]
Alternate sequence: D → N; UniProt: Complete loss of motility.
Mutagenesis-Variant 205
[Blair91a, UniProt11]
Alternate sequence: E → K; UniProt: Decreased motility, subnormal torque, tethered strains rotate very slowly, maybe reduced affinity for the motor.
Mutagenesis-Variant 214
[Blair91a, UniProt11]
Alternate sequence: S → F; UniProt: Complete loss of motility.
Mutagenesis-Variant 217
[Blair91a, UniProt11]
Alternate sequence: R → W; UniProt: Complete loss of motility.
Mutagenesis-Variant 222
[Blair91a, UniProt11]
Alternate sequence: R → H; UniProt: Complete loss of motility.
Mutagenesis-Variant 240
[Blair91a, UniProt11]
Alternate sequence: G → D; UniProt: Decreased motility, subnormal torque, tethered strains rotate very slowly.
Mutagenesis-Variant 242
[Blair91a, UniProt11]
Alternate sequence: A → V; UniProt: Complete loss of motility.
Alternate sequence: A → T; UniProt: Complete loss of motility.
Mutagenesis-Variant 258
[Blair91a, UniProt11]
Alternate sequence: R → H; UniProt: Complete loss of motility.
Alternate sequence: R → C; UniProt: Complete loss of motility.


Gene Local Context (not to scale): ?

Transcription Unit:

Notes:

History:
10/20/97 Gene b1889 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10602; 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

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

Blair91: Blair DF, Berg HC (1991). "Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction." J Mol Biol 221(4);1433-42. PMID: 1719217

Blair91a: Blair DF, Kim DY, Berg HC (1991). "Mutant MotB proteins in Escherichia coli." J Bacteriol 173(13);4049-55. PMID: 2061285

Braun01: Braun TF, Blair DF (2001). "Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex." Biochemistry 40(43);13051-9. PMID: 11669643

Braun04: Braun TF, Al-Mawsawi LQ, Kojima S, Blair DF (2004). "Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli." Biochemistry 43(1);35-45. PMID: 14705929

Chun88: Chun SY, Parkinson JS (1988). "Bacterial motility: membrane topology of the Escherichia coli MotB protein." Science 239(4837);276-8. PMID: 2447650

Fraser99: 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

Garza95: Garza AG, Harris-Haller LW, Stoebner RA, Manson MD (1995). "Motility protein interactions in the bacterial flagellar motor." Proc Natl Acad Sci U S A 92(6);1970-4. PMID: 7892209

Garza96: Garza AG, Biran R, Wohlschlegel JA, Manson MD (1996). "Mutations in motB suppressible by changes in stator or rotor components of the bacterial flagellar motor." J Mol Biol 258(2);270-85. PMID: 8627625

Garza96a: Garza AG, Bronstein PA, Valdez PA, Harris-Haller LW, Manson MD (1996). "Extragenic suppression of motA missense mutations of Escherichia coli." J Bacteriol 178(21);6116-22. PMID: 8892808

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

Grunenfelder03: Grunenfelder B, Gehrig S, Jenal U (2003). "Role of the cytoplasmic C terminus of the FliF motor protein in flagellar assembly and rotation." J Bacteriol 185(5);1624-33. PMID: 12591880

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

Jones90: Jones CJ, Macnab RM, Okino H, Aizawa S (1990). "Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium." J Mol Biol 212(2);377-87. PMID: 2181149

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

Katayama96: Katayama E, Shiraishi T, Oosawa K, Baba N, Aizawa S (1996). "Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images." J Mol Biol 255(3);458-75. PMID: 8568890

Khan88: Khan S, Dapice M, Reese TS (1988). "Effects of mot gene expression on the structure of the flagellar motor." J Mol Biol 202(3);575-84. PMID: 3050128

Kim08: Kim EA, Price-Carter M, Carlquist WC, Blair DF (2008). "Membrane segment organization in the stator complex of the flagellar motor: implications for proton flow and proton-induced conformational change." Biochemistry 47(43);11332-9. PMID: 18834143

Kojima04: Kojima S, Blair DF (2004). "Solubilization and purification of the MotA/MotB complex of Escherichia coli." Biochemistry 43(1);26-34. PMID: 14705928

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

Leake06: Leake MC, Chandler JH, Wadhams GH, Bai F, Berry RM, Armitage JP (2006). "Stoichiometry and turnover in single, functioning membrane protein complexes." Nature 443(7109);355-8. PMID: 16971952

Lele13: Lele PP, Hosu BG, Berg HC (2013). "Dynamics of mechanosensing in the bacterial flagellar motor." Proc Natl Acad Sci U S A 110(29);11839-44. PMID: 23818629

Macnab03: Macnab RM (2003). "How bacteria assemble flagella." Annu Rev Microbiol 57;77-100. PMID: 12730325

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

Minamino00: Minamino T, Yamaguchi S, Macnab RM (2000). "Interaction between FliE and FlgB, a proximal rod component of the flagellar basal body of Salmonella." J Bacteriol 182(11);3029-36. PMID: 10809679

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

Mirel92: Mirel DB, Lustre VM, Chamberlin MJ (1992). "An operon of Bacillus subtilis motility genes transcribed by the sigma D form of RNA polymerase." J Bacteriol 1992;174(13);4197-204. PMID: 1624413

Morimoto14: Morimoto YV, Minamino T (2014). "Structure and function of the bi-directional bacterial flagellar motor." Biomolecules 4(1);217-34. PMID: 24970213

Reid06: Reid SW, Leake MC, Chandler JH, Lo CJ, Armitage JP, Berry RM (2006). "The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11." Proc Natl Acad Sci U S A 103(21);8066-71. PMID: 16698936

Ridgway77: Ridgway HG, Silverman M, Simon MI (1977). "Localization of proteins controlling motility and chemotaxis in Escherichia coli." J Bacteriol 132(2);657-65. PMID: 334749

SaijoHamano04: Saijo-Hamano Y, Uchida N, Namba K, Oosawa K (2004). "In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella." J Mol Biol 339(2);423-35. PMID: 15136044

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

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Other References Related to Gene Regulation

De02: De Wulf P, McGuire AM, Liu X, Lin EC (2002). "Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli." J Biol Chem 277(29);26652-61. PMID: 11953442

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Ide99: Ide N, Ikebe T, Kutsukake K (1999). "Reevaluation of the promoter structure of the class 3 flagellar operons of Escherichia coli and Salmonella." Genes Genet Syst 74(3);113-6. PMID: 10586520

Ko00a: Ko M, Park C (2000). "Two novel flagellar components and H-NS are involved in the motor function of Escherichia coli." J Mol Biol 303(3);371-82. PMID: 11031114

Park01: Park K, Choi S, Ko M, Park C (2001). "Novel sigmaF-dependent genes of Escherichia coli found using a specified promoter consensus." FEMS Microbiol Lett 2001;202(2);243-50. PMID: 11520622

Yu06: Yu HH, Di Russo EG, Rounds MA, Tan M (2006). "Mutational analysis of the promoter recognized by Chlamydia and Escherichia coli sigma(28) RNA polymerase." J Bacteriol 188(15);5524-31. PMID: 16855242

Yu06a: Yu HH, Kibler D, Tan M (2006). "In Silico Prediction and Functional Validation of {sigma}28-Regulated Genes in Chlamydia and Escherichia coli." J Bacteriol 188(23);8206-8212. PMID: 16997971

Zahrl06: Zahrl D, Wagner M, Bischof K, Koraimann G (2006). "Expression and assembly of a functional type IV secretion system elicit extracytoplasmic and cytoplasmic stress responses in Escherichia coli." J Bacteriol 188(18);6611-21. PMID: 16952953


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
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