Q9HUK7 · FIMW_PSEAE
- ProteinCyclic-di-GMP receptor FimW
- GenefimW
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids607 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
High-affinity cyclic-di-GMP binding protein that regulates type IV pili (T4P) elongation. Required for T4P-mediated surface attachment and walking motility during the early phases of surface colonization. Not required for twitching motility. Does not bind related nucleotides such as GMP, GDP, GTP or ATP.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | nucleotide binding |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCyclic-di-GMP receptor FimW
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Pseudomonadales > Pseudomonadaceae > Pseudomonas
Accessions
- Primary accessionQ9HUK7
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Rapidly localizes to the cell poles upon surface contact in a c-di-GMP-dependent manner. Dynamically transitions between the cytoplasm and the cell poles, as a function of c-di-GMP binding.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutant has reduced surface piliation and is unable to increase piliation upon surface exposure. It shows defects in initial surface attachment and in early biofilm formation, but late biofilm formation is not affected. Mutant loses walking motility but twitching motility is barely affected.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 324 | 5.6-fold decrease in c-di-GMP affinity. | ||||
Sequence: R → A | ||||||
Mutagenesis | 328 | Cannot bind c-di-GMP. Fails to localize to the poles and to attach to the surface. | ||||
Sequence: R → A | ||||||
Mutagenesis | 437 | 9.3-fold decrease in c-di-GMP affinity. | ||||
Sequence: S → A | ||||||
Mutagenesis | 440 | Cannot bind c-di-GMP. | ||||
Sequence: G → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000446520 | 1-607 | Cyclic-di-GMP receptor FimW | |||
Sequence: MENQSPHLSLRVPTPTQQNLSFCDATPKDIKYWLAHLPKANLGETARQLYQGLIELNQLVLPVEARLQLLELFRPEVHFVCAHLERHFLNQAIVLDERPRKIANLCQALQNHLAIGYKLIVVQEAPRNSRDRAQLFAVGIQRAIRSLCGPLIRASQLYCPVPEGLWLELHQLYQLASQRGVHRLAVRDELAKHTPGLSVEQAYLIPLLLGCARCNQMRQNNIARLAEVLEPWSQLLSIQSATLPGSLFIAVPQIDGPPRYRSLYPETQLASALGIDTQPLVELIREYLLQPEAERAKARLPLIEGVTLDLLQHLSSAWGDIAERTFQRTQGQGQLTLCIGMSALHYFLAGRRPFNEVLQIQEAPEAPRFKADVQDAWAGAFDAQKVTDWQPGMPLEEIEYRPHQSPRSVQPGHPQAHAQADATEDYPTYALPIVNHSPGGYCLSWPKEVPAQLQAGELVGLQDLPGQAWSIAVVRWIRQVRNGGTQMGIEMIAPAAQPCGLQLLRKTEQSSHYLRALLLPAIAAISRPATVITPRLPFQEGSRVQINLHGEERRAVLNRRQASTGSFSQFEYRSAEPVNTPSDKPVTAPVARPPAGEEDFDSLWKSL |
Proteomic databases
Interaction
Subunit
Monomer in the absence of c-di-GMP. Forms dimers in the presence of c-di-GMP.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 323-492 | PilZ-like domain | ||||
Sequence: ERTFQRTQGQGQLTLCIGMSALHYFLAGRRPFNEVLQIQEAPEAPRFKADVQDAWAGAFDAQKVTDWQPGMPLEEIEYRPHQSPRSVQPGHPQAHAQADATEDYPTYALPIVNHSPGGYCLSWPKEVPAQLQAGELVGLQDLPGQAWSIAVVRWIRQVRNGGTQMGIEMI | ||||||
Motif | 324-328 | RXXXR motif | ||||
Sequence: RTFQR | ||||||
Motif | 435-440 | D/NXSXXG motif | ||||
Sequence: NHSPGG | ||||||
Region | 568-607 | Disordered | ||||
Sequence: SQFEYRSAEPVNTPSDKPVTAPVARPPAGEEDFDSLWKSL |
Domain
Contains a PilZ-like fold that binds two molecules of c-di-GMP via two well-conserved c-di-GMP-binding motifs, RXXXR and D/NXSXXG.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length607
- Mass (Da)67,829
- Last updated2019-04-10 v2
- ChecksumC1A1B553D1D66882
Sequence caution
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE004091 EMBL· GenBank· DDBJ | AAG08343.1 EMBL· GenBank· DDBJ | Genomic DNA | Different initiation |