A0A4D6YBQ8 · A0A4D6YBQ8_BUCMH
- ProteinChaperone protein HtpG
- GenehtpG
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids624 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Molecular chaperone. Has ATPase activity.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 35 | ATP (UniProtKB | ChEBI) | |||
Binding site | 39 | ATP (UniProtKB | ChEBI) | |||
Binding site | 81 | ATP (UniProtKB | ChEBI) | |||
Binding site | 86 | ATP (UniProtKB | ChEBI) | |||
Binding site | 94 | ATP (UniProtKB | ChEBI) | |||
Binding site | 100 | ATP (UniProtKB | ChEBI) | |||
Binding site | 101-102 | ATP (UniProtKB | ChEBI) | |||
Binding site | 175 | ATP (UniProtKB | ChEBI) | |||
Binding site | 335 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | ATP-dependent protein folding chaperone | |
Molecular Function | unfolded protein binding | |
Biological Process | DNA damage response | |
Biological Process | response to heat |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameChaperone protein HtpG
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Erwiniaceae > Buchnera
Accessions
- Primary accessionA0A4D6YBQ8
Proteomes
Subcellular Location
Interaction
Subunit
Homodimer.
Structure
Family & Domains
Sequence
- Sequence statusComplete
- Length624
- Mass (Da)72,980
- Last updated2019-07-31 v1
- Checksum7B9CBA1D40F6F390
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP033004 EMBL· GenBank· DDBJ | QCI23444.1 EMBL· GenBank· DDBJ | Genomic DNA |