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Escherichia coli K-12 substr. MG1655 Protein: Flagellar Export Apparatus

Component of: Flagellum (extended summary available)

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)

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].

Gene-Reaction Schematic: ?

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 [Kutsukake94a].

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


Subunit of Flagellar Export Apparatus: flagellar biosynthesis protein FlhA

Synonyms: FlaH, FlhA

Gene: flhA Accession Numbers: G370 (EcoCyc), b1879, ECK1880

Locations: inner membrane

Sequence Length: 692 AAs

Molecular Weight: 74.843 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0044780 - bacterial-type flagellum assembly Inferred from experiment Inferred by computational analysis [GOA01, Suzuki81]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

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

Unification Links: EcoliWiki:b1879 , PR:PRO_000022650 , Pride:P76298 , Protein Model Portal:P76298 , RefSeq:NP_416393 , SMR:P76298 , String:511145.b1879 , UniProt:P76298

Relationship Links: InterPro:IN-FAMILY:IPR001712 , InterPro:IN-FAMILY:IPR006301 , InterPro:IN-FAMILY:IPR025505 , Pfam:IN-FAMILY:PF00771 , Prints:IN-FAMILY:PR00949 , Prosite:IN-FAMILY:PS00994

Summary:
FlhA is one of six integral membrane components of the flagellar export apparatus. FlhA has two regions: the hydrophobic N-terminal transmembrane region with eight membrane-spanning segments and the C-terminal cytoplasmic domain [Kutsukake94a]. The structures of the C-terminal domain of FlhA and a fragment of the domain have been determined by X-ray crystallography to a resolution of 2.9 and 3.2 Å, respectively [SaijoHamano05]. Temperature-sensitive mutations in the cytoplasmic region of FlhA can prevent flagellar export [Minamino00].

FlhA is osmosensitive and is involved in the stress response at pH 6.5 or lower [Trchounian13].

Essentiality data for flhA 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: flagellar biosynthesis protein FlhB

Synonyms: YecQ, FlaG, FlhB

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

Locations: inner membrane

Sequence Length: 382 AAs

Molecular Weight: 42.238 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

MultiFun Terms: cell structure flagella
cell structure membrane

Unification Links: EcoliWiki:b1880 , PR:PRO_000022651 , Pride:P76299 , Protein Model Portal:P76299 , RefSeq:NP_416394 , 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

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 [Kutsukake94a].

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: flagellar biosynthesis protein FliO

Synonyms: FlbD, FliO

Gene: fliO Accession Numbers: EG11224 (EcoCyc), b1947, ECK1945

Locations: inner membrane, cell projection

Sequence Length: 121 AAs

Molecular Weight: 12.67 kD (from nucleotide sequence)

Molecular Weight: 13 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [GOA01]
GO:0097588 - archaeal or bacterial-type flagellum-dependent cell motility Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

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

Unification Links: EcoliWiki:b1947 , Pride:P22586 , Protein Model Portal:P22586 , RefSeq:NP_416457 , String:511145.b1947 , UniProt:P22586

Relationship Links: InterPro:IN-FAMILY:IPR022781 , Pfam:IN-FAMILY:PF04347

Summary:
FliO is one of six integral membrane components of the flagellar export apparatus [Minamino04]. FliO has a small N-terminal cytoplasmic domain, a hydrophobic domain consisting of a single transmembrane helix and a considerable periplasmic domain [Minamino99].

Essentiality data for fliO 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: flagellar biosynthesis protein FliP

Synonyms: FlaR, FliP

Gene: fliP Accession Numbers: EG11975 (EcoCyc), b1948, ECK1946

Locations: inner membrane, cell projection

Sequence Length: 245 AAs

Molecular Weight: 26.928 kD (from nucleotide sequence)

Molecular Weight: 25 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Zhang07, Daley05]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a]

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

Unification Links: EcoliWiki:b1948 , PR:PRO_000022666 , Protein Model Portal:P0AC05 , RefSeq:NP_416458 , String:511145.b1948 , UniProt:P0AC05

Relationship Links: InterPro:IN-FAMILY:IPR005837 , InterPro:IN-FAMILY:IPR005838 , Pfam:IN-FAMILY:PF00813 , Prints:IN-FAMILY:PR00951 , Prints:IN-FAMILY:PR01302 , Prosite:IN-FAMILY:PS01060 , Prosite:IN-FAMILY:PS01061

Summary:
FliP is one of six integral membrane components of the flagellar export apparatus [Minamino04, Fan97a]. FliP has a substantial periplasmic domain between two of its four transmembrane domains [Minamino99].

Essentiality data for fliP 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: flagellar biosynthesis protein FliQ

Synonyms: FlaQ, FliQ

Gene: fliQ Accession Numbers: EG11976 (EcoCyc), b1949, ECK1947

Locations: inner membrane, cell projection

Sequence Length: 89 AAs

Molecular Weight: 9.632 kD (from nucleotide sequence)

Molecular Weight: 10 kD (experimental) [Malakooti94]

GO Terms:

Biological Process: GO:0009306 - protein secretion Inferred by computational analysis [GOA01]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

MultiFun Terms: cell structure flagella
metabolism biosynthesis of macromolecules (cellular constituents) flagellum
metabolism biosynthesis of macromolecules (cellular constituents) glycoprotein

Unification Links: EcoliWiki:b1949 , Protein Model Portal:P0AC07 , RefSeq:NP_416459 , String:511145.b1949 , UniProt:P0AC07

Relationship Links: InterPro:IN-FAMILY:IPR002191 , InterPro:IN-FAMILY:IPR006305 , Pfam:IN-FAMILY:PF01313 , Prints:IN-FAMILY:PR00952

Summary:
FliQ is one of six integral membrane components of the flagellar export apparatus [Minamino04]. FliQ has two transmembrane domains [Minamino99].

Essentiality data for fliQ 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: flagellar biosynthesis protein FliR

Synonyms: FlaP, FliR

Gene: fliR Accession Numbers: EG11977 (EcoCyc), b1950, ECK1948

Locations: inner membrane, cell projection

Sequence Length: 261 AAs

Molecular Weight: 28.543 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006605 - protein targeting Inferred by computational analysis [GOA01]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred from experiment Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, DiazMejia09, Daley05]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [UniProtGOA11a]
GO:0009425 - bacterial-type flagellum basal body Inferred by computational analysis [UniProtGOA11]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016021 - integral component of membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

MultiFun Terms: cell structure flagella
transport Putative uncharacterized transport protein

Unification Links: EcoliWiki:b1950 , PR:PRO_000022667 , Protein Model Portal:P33135 , RefSeq:NP_416460 , String:511145.b1950 , UniProt:P33135

Relationship Links: InterPro:IN-FAMILY:IPR002010 , InterPro:IN-FAMILY:IPR006303 , Pfam:IN-FAMILY:PF01311 , Prints:IN-FAMILY:PR00953

Summary:
FliR is one of six integral membrane components of the flagellar export apparatus [Minamino04, Fan97a]. FliR has five or six transmembrane helices connected by short loops [Ohnishi97].

Essentiality data for fliR 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: flagellar biosynthesis protein FliH

Synonyms: FliH

Gene: fliH Accession Numbers: EG11656 (EcoCyc), b1940, ECK1938

Locations: cytosol, cell projection

Sequence Length: 228 AAs

Molecular Weight: 25.05 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum 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

Unification Links: DIP:DIP-9654N , EcoliWiki:b1940 , PR:PRO_000022659 , Protein Model Portal:P31068 , RefSeq:NP_416450 , String:511145.b1940 , UniProt:P31068

Relationship Links: InterPro:IN-FAMILY:IPR000563 , InterPro:IN-FAMILY:IPR018035 , Pfam:IN-FAMILY:PF02108 , Prints:IN-FAMILY:PR01003

Summary:
FliH is a cytoplasmic protein which exists as a dimer in solution and forms a stable heterotrimeric complex with FliI, inhibiting its ATPase activity [Minamino00a].

Essentiality data for fliH 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: flagellum-specific ATP synthase FliI

Synonyms: Fla, FlaC, FliI

Gene: fliI Accession Numbers: G377 (EcoCyc), b1941, ECK1939

Locations: inner membrane, cytosol

Sequence Length: 457 AAs

Molecular Weight: 49.316 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006200 - ATP catabolic process Inferred by computational analysis [GOA01]
GO:0006754 - ATP biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006811 - ion transport Inferred by computational analysis [UniProtGOA11a]
GO:0009058 - biosynthetic process Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0015992 - proton transport Inferred by computational analysis [UniProtGOA11a]
GO:0030254 - protein secretion by the type III secretion system Inferred by computational analysis [GOA01]
GO:0044780 - bacterial-type flagellum assembly Inferred by computational analysis [GOA01]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01]
Molecular Function: GO:0042802 - identical protein binding Inferred from experiment [Marykwas96, Rajagopala14, Rajagopala09]
GO:0000166 - nucleotide binding Inferred by computational analysis [UniProtGOA11a]
GO:0005524 - ATP binding Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016887 - ATPase activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA01]
GO:0005886 - plasma membrane Inferred by computational analysis [DiazMejia09]
GO:0030257 - type III protein secretion system complex Inferred by computational analysis [GOA01]

MultiFun Terms: cell structure flagella
metabolism energy metabolism, carbon ATP proton motive force interconversion

Unification Links: DIP:DIP-9655N , EcoliWiki:b1941 , ModBase:P52612 , PR:PRO_000022660 , Pride:P52612 , Protein Model Portal:P52612 , RefSeq:NP_416451 , SMR:P52612 , String:511145.b1941 , UniProt:P52612

Relationship Links: InterPro:IN-FAMILY:IPR000194 , InterPro:IN-FAMILY:IPR003593 , InterPro:IN-FAMILY:IPR005714 , InterPro:IN-FAMILY:IPR020003 , InterPro:IN-FAMILY:IPR020005 , InterPro:IN-FAMILY:IPR027417 , Panther:IN-FAMILY:PTHR15184:SF9 , Pfam:IN-FAMILY:PF00006 , Prosite:IN-FAMILY:PS00152 , Smart:IN-FAMILY:SM00382

Summary:
FliI is a cytoplasmic component of the flagellar export apparatus and serves as the ATPase of the apparatus, providing the energy for translocation of export substrates across the cytoplasmic membrane [Fan96]. The structure of FliI missing the N-terminal 18 amino acids was determined by X-ray crystallography to a resolution of 2.4 Å [Minamino06b].

Essentiality data for fliI 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: flagellar biosynthesis protein FliJ

Synonyms: FlaO, FliJ

Gene: fliJ Accession Numbers: G378 (EcoCyc), b1942, ECK1940

Locations: inner membrane, cell projection

Sequence Length: 147 AAs

Molecular Weight: 17.307 kD (from nucleotide sequence)

GO Terms:

Biological Process: GO:0006810 - transport Inferred by computational analysis [UniProtGOA11a]
GO:0006935 - chemotaxis Inferred by computational analysis [UniProtGOA11a, GOA01]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01]
GO:0015031 - protein transport Inferred by computational analysis [UniProtGOA11a]
GO:0044781 - bacterial-type flagellum organization Inferred by computational analysis [UniProtGOA11a]
GO:0071973 - bacterial-type flagellum-dependent cell motility Inferred by computational analysis [GOA01]
Molecular Function: GO:0003774 - motor activity Inferred by computational analysis [GOA01]
Cellular Component: GO:0005886 - plasma membrane Inferred by computational analysis [UniProtGOA11, UniProtGOA11a]
GO:0009288 - bacterial-type flagellum Inferred by computational analysis [GOA01]
GO:0016020 - membrane Inferred by computational analysis [UniProtGOA11a, GOA01]

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

Unification Links: DIP:DIP-9656N , EcoliWiki:b1942 , Mint:MINT-1258288 , PR:PRO_000022661 , Pride:P52613 , Protein Model Portal:P52613 , RefSeq:NP_416452 , SMR:P52613 , String:511145.b1942 , UniProt:P52613

Relationship Links: InterPro:IN-FAMILY:IPR012823 , InterPro:IN-FAMILY:IPR018006 , Pfam:IN-FAMILY:PF02050 , Prints:IN-FAMILY:PR01004

Summary:
FliJ is one of three soluble components of the flagellar export system, along with FliH and FliI [Minamino99]. FliJ has several feature similarities with the type III cytoplasmic chaperone family [Minamino04].

Essentiality data for fliJ knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
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]

References

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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 Dec 18, 2014, biocyc13.