A1AUF5 · HSLO_PELPD
- Protein33 kDa chaperonin
- GenehslO
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids304 (go to sequence)
- Protein existenceInferred from homology
- Annotation score2/5
Function
function
Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress.
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 | protein folding chaperone | |
Molecular Function | unfolded protein binding | |
Biological Process | protein refolding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended name33 kDa chaperonin
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Desulfuromonadaceae > Pelobacter
Accessions
- Primary accessionA1AUF5
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for chain, disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_1000015553 | 1-304 | 33 kDa chaperonin | |||
Sequence: MGDHIIRSLSVSGGIRILVCDVALLTREICRLHGASPTVSIALGRGLAGGALMGALLKPGQRLALKFEANGPLRKMIVEADSDGAVRASVANPTAEAEPLEGRWNVAGVLGRAGFLTVSKDLGLGGQPYQGTVQLCSSEIGDDLAYYLADSEQTPSAVGLGAALDEDGLISVCGGFLVQALPGVDEAERDRVTDNIASLPPLSSLLREGGTQKLLELLFDSVAYTRLETRELFFRCGCGREKVERALLSLGGAELWDMGTREGEARVTCEFCRQSYQFDADELKALAETATLTRIHEEHEHLQQ | ||||||
Disulfide bond | 236↔238 | Redox-active | ||||
Sequence: CGC | ||||||
Disulfide bond | 269↔272 | Redox-active | ||||
Sequence: CEFC |
Post-translational modification
Under oxidizing conditions two disulfide bonds are formed involving the reactive cysteines. Under reducing conditions zinc is bound to the reactive cysteines and the protein is inactive.
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length304
- Mass (Da)32,453
- Last updated2007-01-23 v1
- Checksum3D38290FB8F8D5BF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000482 EMBL· GenBank· DDBJ | ABL00976.1 EMBL· GenBank· DDBJ | Genomic DNA |