Protein profile

PA1105

flagellar biosynthesis chaperone

Genome: NC_002516.2

Gene: fliJ PA1105 Structure source: AlphaFold UniProt Q9I4N0
Amino acids 147
Annotations 8
Features 22
PDB binders 0

Overview

Basic information about this protein and its source genome.

Accession
PA1105
Gene
fliJ PA1105
Status
annotated
Amino acids
147
Structure source
AlphaFold

Target profile

Computed evidence for target prioritization.

Human off-target
No hit
Gut microbiome off-target
hit
Essential (DEG)
N
Localization
Cytoplasmic

Sequence

Primary amino-acid sequence viewer.

Functional Annotations

Enzyme classification and Gene Ontology terms linked to this protein.

8 GO

Gene Ontology (GO)

8
  • GO:0009288 A motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.
  • GO:0005886 The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
  • GO:0003774 Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force).
  • GO:0044781 A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a bacterial-type flagellum, a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope which functions in cell motility.
  • GO:0071973 Cell motility due to the motion of one or more bacterial-type flagella. A bacterial-type flagellum is a motor complex composed of an extracellular helical protein filament coupled to a rotary motor embedded in the cell envelope.
  • GO:0006935 The directed movement of a motile cell or organism, or the directed growth of a cell guided by a specific chemical concentration gradient. Movement may be towards a higher concentration (positive chemotaxis) or towards a lower concentration (negative chemotaxis).
  • GO:0015031 The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.
  • GO:0016020 A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it.

Sequence Features

Domain/signature hits from InterPro and related databases.

22 records
Show feature table
Start End DB Term Name
1 147 PIRSF PIRSF019404 FliJ
1 147 InterPro IPR018006 Flagellar FliJ, proteobacteria
1 146 PANTHER PTHR38786 FLAGELLAR FLIJ PROTEIN
21 141 Pfam PF02050 Flagellar FliJ protein
21 141 InterPro IPR012823 Flagellar export FliJ
26 53 Coils Coil Coil
6 141 NCBIfam TIGR02473 flagellar export protein FliJ
6 141 InterPro IPR012823 Flagellar export FliJ
109 136 Coils Coil Coil
5 27 PRINTS PR01004 Flagellar FliJ protein signature
5 27 InterPro IPR018006 Flagellar FliJ, proteobacteria
64 85 PRINTS PR01004 Flagellar FliJ protein signature
64 85 InterPro IPR018006 Flagellar FliJ, proteobacteria
109 127 PRINTS PR01004 Flagellar FliJ protein signature
109 127 InterPro IPR018006 Flagellar FliJ, proteobacteria
87 108 PRINTS PR01004 Flagellar FliJ protein signature
87 108 InterPro IPR018006 Flagellar FliJ, proteobacteria
45 62 PRINTS PR01004 Flagellar FliJ protein signature
45 62 InterPro IPR018006 Flagellar FliJ, proteobacteria
127 147 PRINTS PR01004 Flagellar FliJ protein signature
127 147 InterPro IPR018006 Flagellar FliJ, proteobacteria
1 146 Gene3D G3DSA:1.10.287.1700 -

3D Structure

Selected loaded structure. Experimental PDB entries may cover only a portion of the sequence; predicted models typically cover the full protein.

3D visualization script Full viewer

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Structural evidence

0 + 1

Experimental PDB entries and predicted models. Click Switch to display a different structure in the viewer.

Entry Method Resolution Chain Coverage Links Status
AlphaFold PA1105
AlphaFold full sequence Viewing