P94337
Gene name |
ftsZ |
Protein name |
Cell division protein FtsZ |
Names |
|
Species |
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025) |
KEGG Pathway |
cgl:Cgl2155 |
EC number |
|
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
4 structures for P94337
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 6SAT | X-ray | 160 A | P/Q | 433-442 | PDB |
| 6SCS | X-ray | 220 A | P/Q/R/S | 433-442 | PDB |
| 8BVF | X-ray | 268 A | C/D | 433-442 | PDB |
| AF-P94337-F1 | Predicted | AlphaFoldDB |
No variants for P94337
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P94337 | |||||
No associated diseases with P94337
6 regional properties for P94337
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tubulin/FtsZ, GTPase domain | 10 - 208 | IPR003008-1 |
| domain | Tubulin/FtsZ, GTPase domain | 209 - 230 | IPR003008-2 |
| domain | Tubulin/FtsZ, 2-layer sandwich domain | 204 - 321 | IPR018316 |
| conserved_site | Cell division protein FtsZ, conserved site | 41 - 75 | IPR020805-1 |
| conserved_site | Cell division protein FtsZ, conserved site | 94 - 115 | IPR020805-2 |
| domain | Cell division protein FtsZ, C-terminal | 219 - 313 | IPR024757 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cell division site | The eventual plane of cell division (also known as cell cleavage or cytokinesis) in a dividing cell. In Eukaryotes, the cleavage apparatus, composed of septin structures and the actomyosin contractile ring, forms along this plane, and the mitotic, or meiotic, spindle is aligned perpendicular to the division plane. In bacteria, the cell division site is generally located at mid-cell and is the site at which the cytoskeletal structure, the Z-ring, assembles. |
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| division septum assembly | The assembly and arrangement of a septum that spans the plasma membrane interface between progeny cells following cytokinesis. The progeny cells that form a division septum are not able to exchange intracellular material. |
| FtsZ-dependent cytokinesis | A cytokinesis process that involves a set of conserved proteins including FtsZ, and results in the formation of two similarly sized and shaped cells. |
| protein polymerization | The process of creating protein polymers, compounds composed of a large number of component monomers; polymeric proteins may be made up of different or identical monomers. Polymerization occurs by the addition of extra monomers to an existing poly- or oligomeric protein. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTSPNNYLAK | IKVVGVGGGG | VNAVNRMIEE | GLKGVEFIAV | NTDSQALMFS | DADVKLDIGR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EATRGLGAGA | NPEVGRASAE | DHKNEIEETI | KGADMVFVTA | GEGGGTGTGA | APVVAGIAKK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| MGALTIGVVT | KPFEFEGRRR | TRQAEEGIAA | LKEVCDTLIV | IPNDRLLELG | DANLSIMEAF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RAADEVLHNG | VQGITNLITI | PGVINVDFAD | VRSVMSEAGS | ALMGVGSARG | DNRVVSATEQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AINSPLLEAT | MDGATGVLLS | FAGGSDLGLM | EVNAAASMVR | ERSDEDVNLI | FGTIIDDNLG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DEVRVTVIAT | GFDAARASAA | ENRRAGISAA | PAAEPVQQQV | PTTNATLPPE | KESIFGGARE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ENDPYLSRSA | GARHRIEETR | SGGGLFTTGN | DRDYRRDERR | EDHRDERRDE | RRDDRSYDRR |
| 430 | 440 | ||||
| DDRRDDRRDD | RGDDLDVPSF | LQ |