Q9WZP2
Gene name |
enc |
Protein name |
Type 1 encapsulin shell protein |
Names |
Maritimacin, Thermotoga bacteriocin |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM0785 |
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
13 structures for Q9WZP2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 3DKT | X-ray | 310 A | A/B/C/D/E/F/G/H/I/J | 1-265 | PDB |
| 6WKV | EM | 299 A | 0/1/2/3/4/5/6/7/8/9/A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T | 1-265 | PDB |
| 7K5W | EM | 287 A | A | 1-265 | PDB |
| 7KQ5 | EM | 200 A | A | 1-265 | PDB |
| 7LII | EM | 355 A | A | 1-265 | PDB |
| 7LIJ | EM | 284 A | A | 1-265 | PDB |
| 7LIK | EM | 291 A | A | 1-265 | PDB |
| 7LIL | EM | 284 A | A | 1-265 | PDB |
| 7LIM | EM | 275 A | A | 1-265 | PDB |
| 7LIS | EM | 296 A | A | 1-265 | PDB |
| 7LIT | EM | 253 A | A | 1-265 | PDB |
| 7MU1 | EM | 330 A | A | 1-264 | PDB |
| AF-Q9WZP2-F1 | Predicted | AlphaFoldDB |
No variants for Q9WZP2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9WZP2 | |||||
No associated diseases with Q9WZP2
4 regional properties for Q9WZP2
Functions
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| encapsulin nanocompartment | Intracellular non-membrane bound organelle, consisting of proteinaceous polyhedral shells that encapsulate enzymes, protecting the contents from their surrounding milieu and/or the milieu from reactants in their interior. The self-assembling, 25-42 nm nanocompartment shell, unlike larger bacterial microcompartments, is made of only one protein, and has only a few proteins inside. Shells about vary from about 25-42 nm in diameter. The shell protein has an HK97-like fold and probably evolved from a viral protein. Artificial encapsulin nanocompartments can be expressed and filled with cargo proteins for biotechnological uses. They are found in many bacterial and a few archaeal phyla. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| peptidase activity | Catalysis of the hydrolysis of a peptide bond. A peptide bond is a covalent bond formed when the carbon atom from the carboxyl group of one amino acid shares electrons with the nitrogen atom from the amino group of a second amino acid. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular iron ion homeostasis | Any process involved in the maintenance of an internal steady state of iron ions at the level of a cell. |
| ion transport | The directed movement of charged atoms or small charged molecules into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEFLKRSFAP | LTEKQWQEID | NRAREIFKTQ | LYGRKFVDVE | GPYGWEYAAH | PLGEVEVLSD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ENEVVKWGLR | KSLPLIELRA | TFTLDLWELD | NLERGKPNVD | LSSLEETVRK | VAEFEDEVIF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RGCEKSGVKG | LLSFEERKIE | CGSTPKDLLE | AIVRALSIFS | KDGIEGPYTL | VINTDRWINF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LKEEAGHYPL | EKRVEECLRG | GKIITTPRIE | DALVVSERGG | DFKLILGQDL | SIGYEDREKD |
| 250 | 260 | ||||
| AVRLFITETF | TFQVVNPEAL | ILLKF |