P21558
Gene name |
gyrB |
Protein name |
DNA gyrase subunit B |
Names |
|
Species |
Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2) (Haloferax alicantei) |
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 P21558
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P21558-F1 | Predicted | AlphaFoldDB |
No variants for P21558
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P21558 | |||||
No associated diseases with P21558
6 regional properties for P21558
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 487 - 570 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 66 - 250 | IPR000795 |
| domain | Small GTP-binding protein domain | 68 - 235 | IPR005225 |
| domain | GTP-binding protein LepA, C-terminal | 576 - 681 | IPR013842 |
| conserved_site | Tr-type G domain, conserved site | 105 - 120 | IPR031157 |
| domain | Elongation factor 4, domain IV | 489 - 568 | IPR035654 |
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 | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| chromosome | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 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. |
| metal ion binding | Binding to a metal ion. |
3 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. |
| DNA-templated DNA replication | A DNA replication process that uses parental DNA as a template for the DNA-dependent DNA polymerases that synthesize the new strands. |
| response to antibiotic | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an antibiotic stimulus. An antibiotic is a chemical substance produced by a microorganism which has the capacity to inhibit the growth of or to kill other microorganisms. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSQDNEYGAG | QIQVLEGLEA | VRKRPAMYIG | STDSRGLHHL | VYEVVDNSID | EALAGHCDAI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EVALHEDGSV | SVTDNGRGIP | VDTHEQYDRP | ALEVIMTVLH | AGGKFDNKSY | QVSGGLHGVG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VSVVNALSSE | LEVEVKRDGA | VWTHRFEVGE | PQVEEFERVR | DLEPGEDTGT | TIRFWPDDGI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FETTEFDFKT | LENRLRELAF | LNSGVEISLS | DERTDESSTF | LFEGGIREFV | EYLNETKTAL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HDDVIYYDDE | SEGIEVEIAM | QATDELQGSI | HAFANNINTR | EGGTHLTGFK | TALTRVVNDY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ANSHDMLDDL | DGDNLRGEDV | REGLTAVISV | KHPDPQFEGQ | TKTKLGNSEV | RGIVESVTHQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QLGTFFEENP | DTATAIISKA | VEAARARKAA | KQAEELTRRK | SALESTSLPG | KLADCQSRDP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SESELFIVEG | DSAGGSAKQG | RDRKFQAILP | LKGKILNVEK | HRLDRILEND | EIRALITAIG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GGVGDEFDIE | KARYQRLILM | TDADVDGAHI | RTLLLTLLYR | HMRPLIEAGY | VYAAQPPLYR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VRYRGNTYDA | MDEAERDRII | EEECNGNPTQ | VQRFKGLGEM | NPDQLWDTTM | NPENRVLKRI |
| 610 | 620 | 630 | |||
| TVEDAAAADR | MFNILMGDAV | GPRKQFIKDH | ANDAEWVDI |