O30583 · COMP_ACIAD
- ProteinPilin-like competence factor ComP
- GenecomP
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids147 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Pilin-like competence factor, which is essential for natural transformation of the Gram-negative soil bacterium A.baylyi ADP1. Is not a subunit of the pilus structures. Likely functions as a major subunit of an oligomeric structure acting as a channel or pore mediating DNA translocation through the outer membrane and periplasm.
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 | cell outer membrane | |
Cellular Component | periplasmic space | |
Cellular Component | pilus | |
Cellular Component | plasma membrane | |
Molecular Function | DNA binding | |
Biological Process | cell adhesion | |
Biological Process | establishment of competence for transformation |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePilin-like competence factor ComP
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Moraxellales > Moraxellaceae > Acinetobacter
Accessions
- Primary accessionO30583
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Note: The 20-kDa form is present in the cytoplasmic membrane, the periplasm, and the outer membrane, whereas the 23-kDa form is located in the outer membrane and might be due to a further modification.
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
A deletion of comP completely abolishes natural transformation, due to a complete lack of DNA binding and, therefore, uptake of DNA, but has no effect on piliation and on twitching motility.
PTM/Processing
Features
Showing features for propeptide, modified residue, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Propeptide | PRO_0000433788 | 1-6 | |||
Modified residue | 7 | N-methylphenylalanine | |||
Chain | PRO_0000433789 | 7-147 | Pilin-like competence factor ComP | ||
Post-translational modification
Glycosylated by PglL2 (PubMed:23658772).
The 20-kDa form is glycosylated; a 23-kDa form also exists, that might be due to a further modification. The glycosylation of ComP is not required for its function in DNA binding and uptake (PubMed:10850981).
The 20-kDa form is glycosylated; a 23-kDa form also exists, that might be due to a further modification. The glycosylation of ComP is not required for its function in DNA binding and uptake (PubMed:10850981).
Keywords
- PTM
Expression
Induction
Is maximally expressed in the late stationary growth phase (at protein and mRNA level). Minimal comP expression levels are detected in the middle of the logarithmic growth phase.
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length147
- Mass (Da)14,872
- Last updated1998-01-01 v1
- Checksum682DBC062230C479
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF012550 EMBL· GenBank· DDBJ | AAC45886.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CR543861 EMBL· GenBank· DDBJ | CAG70007.1 EMBL· GenBank· DDBJ | Genomic DNA |