P0A2I5 · PARE_SALTY
- ProteinDNA topoisomerase 4 subunit B
- GeneparE
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids630 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA (PubMed:22916023).
Performs the decatenation events required during the replication of a circular DNA molecule
Performs the decatenation events required during the replication of a circular DNA molecule
Catalytic activity
Cofactor
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Ca2+ (UniProtKB | Rhea| CHEBI:29108 )
Note: Binds two Mg2+ per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn2+ or Ca2+.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 5 | ATP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 42 | ATP (UniProtKB | ChEBI) | ||||
Sequence: N | ||||||
Binding site | 69 | ATP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 110-116 | ATP (UniProtKB | ChEBI) | ||||
Sequence: GLHGVGI | ||||||
Binding site | 334 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 418 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Site | 443 | Interaction with DNA | ||||
Sequence: K | ||||||
Site | 446 | Interaction with DNA | ||||
Sequence: N | ||||||
Binding site | 490 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 490 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 492 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 497 | Interaction with DNA | ||||
Sequence: H | ||||||
Site | 615 | Interaction with DNA | ||||
Sequence: R |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | chromosome | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | |
Molecular Function | metal ion binding | |
Biological Process | chromosome segregation | |
Biological Process | DNA topological change |
Keywords
- Molecular function
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA topoisomerase 4 subunit B
- EC number
- Alternative names
Gene names
Organism names
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Salmonella
Accessions
- Primary accessionP0A2I5
- Secondary accessions
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Phenotypes & Variants
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 67 | in temperature-sensitive mutants parE206 and parE374 | ||||
Sequence: V → M | ||||||
Mutagenesis | 67 | In parE206TS; a temperature-sensitive mutant, 33% decreased growth rate, slightly decreased negative supercoiling at permissive temperature. | ||||
Sequence: V → M | ||||||
Natural variant | 399 | in temperature-sensitive mutant parE377 | ||||
Sequence: G → S | ||||||
Natural variant | 583 | in temperature-sensitive mutant parE493 | ||||
Sequence: T → P |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000145429 | 1-630 | DNA topoisomerase 4 subunit B | |||
Sequence: MTQTYNADAIEVLTGLEPVRRRPGMYTDTTRPNHLGQEVIDNSVDEALAGHAKRVDVILHADQSLEVIDDGRGMPVDIHPEEGVPAVELILCRLHAGGKFSNKNYQFSGGLHGVGISVVNALSKRVEVTVRRDGQVYNIAFENGEKVQDLQVVGTCGKRNTGTSVHFWPDESFFDSPRFSVSRLMHVLKAKAVLCPGVEITFKDEVNNSEQRWCYQDGLNDYLGEAVNGLPTLPEKPFIGNFNGETEAVDWALLWLPEGGELLTESYVNLIPTMQGGTHVNGLRQGLLDAMREFCEYRNILPRGVKLSAEDIWDRCAYVLSVKMQDPQFAGQTKERLSSRQCAAFVSGVVKDAFSLWLNQNVQAAEQLAEMAIASAQRRLRAAKKVVRKKLTSGPALPGKLADCTAQDLNRTELFLVEGDSAGGSAKQARDREYQAIMPLKGKILNTWEVSSDEVLASQEVHDISVAIGIDPDSDDLSQLRYGKICILADADSDGLHIATLLCALFVRHFRALVKNGHVYVALPPLYRIDLGKEVYYALTEEEKAGVLEQLKRKKGKPNVQRFKGLGEMNPMQLRETTLDPNTRRLVQLTISDEDDQRTNAMMDMLLAKKRSEDRRNWLQEKGDLADLDV |
Proteomic databases
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 412-525 | Toprim | ||||
Sequence: TELFLVEGDSAGGSAKQARDREYQAIMPLKGKILNTWEVSSDEVLASQEVHDISVAIGIDPDSDDLSQLRYGKICILADADSDGLHIATLLCALFVRHFRALVKNGHVYVALPP |
Sequence similarities
Belongs to the type II topoisomerase family. ParE type 1 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length630
- Mass (Da)70,089
- Last updated2005-03-15 v1
- Checksum7F2FCC25EB830019
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 305 | in Ref. 1; AAA27182 | ||||
Sequence: V → Q | ||||||
Sequence conflict | 333 | in Ref. 1; AAA27182 | ||||
Sequence: T → P | ||||||
Sequence conflict | 383 | in Ref. 1; AAA27182 | ||||
Sequence: A → R |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L05544 EMBL· GenBank· DDBJ | AAA27182.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AE006468 EMBL· GenBank· DDBJ | AAL22055.1 EMBL· GenBank· DDBJ | Genomic DNA |