Q43947
Gene name |
gyrB |
Protein name |
DNA gyrase subunit B |
Names |
|
Species |
Acinetobacter calcoaceticus |
KEGG Pathway |
|
EC number |
5.6.2.2: Enzymes altering nucleic acid conformation |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q43947
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q43947-F1 | Predicted | AlphaFoldDB |
No variants for Q43947
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q43947 | |||||
No associated diseases with Q43947
No regional properties for Q43947
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q43947 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 5.6.2.2 | Enzymes altering nucleic acid conformation |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity | Catalysis of a DNA topological transformation by transiently cleaving a pair of complementary DNA strands to form a gate through which a second double-stranded DNA segment is passed, after which the severed strands in the first DNA segment are rejoined, driven by ATP hydrolysis. The enzyme changes the linking number in multiples of 2. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA topological change | The process in which a transformation is induced in the topological structure of a double-stranded DNA helix, resulting in a change in linking number. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| DNSYKVSGGL | HGVSVSVVNA | LSSKLHLMIS | RAGQVHEQEY | QHGDPQYPLR | VIGETDKSGT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TVRFWPSELT | FTQTIFNVEI | LARRLRELSF | LNAGVRIVLR | DERINLEHVY | DYEGGLSEFV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KYINEGKTHL | NEIFHFTADT | DSGIGVEVAL | QWNESYQENV | RCFTNNIPQK | DGGSHLAGFR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AALTRGLNQY | LENENILKKE | KVNVTGDDAR | EGLTAIISVK | VPDPKFSSQT | KEKLVSSEVK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PAVEQAMNKE | FSAYLLENPQ | AAKSIAGKII | DAARARDAAR | KAREMTRRKS | ALDIAGLPGK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LADCQEKDPA | LSELYLVEGD | SAGGSAKQGR | NRKMQAILPL | KGKILNVERA | RFDKMISSQE |
| 370 | 380 | ||||
| VGTLITALGC | GIGREEYNPD | KLRYHKII |