P07788
Gene name |
cotA |
Protein name |
Laccase |
Names |
Bilirubin oxidase, Spore coat protein A |
Species |
Bacillus subtilis (strain 168) |
KEGG Pathway |
bsu:BSU06300 |
EC number |
1.3.3.5: With oxygen as acceptor |
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
27 structures for P07788
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1GSK | X-ray | 170 A | A | 1-513 | PDB |
| 1OF0 | X-ray | 245 A | A | 1-513 | PDB |
| 1W6L | X-ray | 200 A | A | 1-513 | PDB |
| 1W6W | X-ray | 220 A | A | 1-513 | PDB |
| 1W8E | X-ray | 220 A | A | 1-513 | PDB |
| 2BHF | X-ray | 250 A | A | 1-513 | PDB |
| 2WSD | X-ray | 160 A | A | 1-513 | PDB |
| 2X87 | X-ray | 200 A | A | 1-513 | PDB |
| 2X88 | X-ray | 180 A | A | 1-513 | PDB |
| 3ZDW | X-ray | 245 A | A | 1-513 | PDB |
| 4A66 | X-ray | 195 A | A | 1-513 | PDB |
| 4A67 | X-ray | 210 A | A | 1-513 | PDB |
| 4A68 | X-ray | 200 A | A | 1-513 | PDB |
| 4AKO | X-ray | 170 A | A | 1-513 | PDB |
| 4AKP | X-ray | 200 A | A | 1-513 | PDB |
| 4AKQ | X-ray | 210 A | A | 1-513 | PDB |
| 4Q89 | X-ray | 231 A | A/B | 1-513 | PDB |
| 4Q8B | X-ray | 191 A | A/B | 1-513 | PDB |
| 4YVN | X-ray | 230 A | A | 1-513 | PDB |
| 4YVU | X-ray | 230 A | A | 1-513 | PDB |
| 5ZLJ | X-ray | 196 A | A | 1-513 | PDB |
| 5ZLK | X-ray | 260 A | A | 1-513 | PDB |
| 5ZLL | X-ray | 260 A | A | 1-513 | PDB |
| 5ZLM | X-ray | 170 A | A | 1-513 | PDB |
| 7Y8B | X-ray | 200 A | A/B | 1-513 | PDB |
| 7Y8C | X-ray | 200 A | A/B | 1-513 | PDB |
| AF-P07788-F1 | Predicted | AlphaFoldDB |
No variants for P07788
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P07788 | |||||
No associated diseases with P07788
4 regional properties for P07788
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Multicopper oxidase, second cupredoxin domain | 240 - 318 | IPR001117 |
| domain | Multicopper oxidase, C-terminal | 378 - 509 | IPR011706 |
| domain | Multicopper oxidase, N-terminal | 45 - 81 | IPR011707-1 |
| domain | Multicopper oxidase, N-terminal | 101 - 178 | IPR011707-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.3.5 | With oxygen as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| outer membrane-bounded periplasmic space | The region between the inner (cytoplasmic or plasma) membrane and outer membrane of organisms with two membranes such as Gram negative bacteria. These periplasmic spaces are relatively thick and contain a thin peptidoglycan layer (PGL), also referred to as a thin cell wall. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| copper ion binding | Binding to a copper (Cu) ion. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| sporulation resulting in formation of a cellular spore | The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTLEKFVDAL | PIPDTLKPVQ | QSKEKTYYEV | TMEECTHQLH | RDLPPTRLWG | YNGLFPGPTI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EVKRNENVYV | KWMNNLPSTH | FLPIDHTIHH | SDSQHEEPEV | KTVVHLHGGV | TPDDSDGYPE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AWFSKDFEQT | GPYFKREVYH | YPNQQRGAIL | WYHDHAMALT | RLNVYAGLVG | AYIIHDPKEK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLKLPSDEYD | VPLLITDRTI | NEDGSLFYPS | APENPSPSLP | NPSIVPAFCG | ETILVNGKVW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PYLEVEPRKY | RFRVINASNT | RTYNLSLDNG | GDFIQIGSDG | GLLPRSVKLN | SFSLAPAERY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DIIIDFTAYE | GESIILANSA | GCGGDVNPET | DANIMQFRVT | KPLAQKDESR | KPKYLASYPS |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VQHERIQNIR | TLKLAGTQDE | YGRPVLLLNN | KRWHDPVTET | PKVGTTEIWS | IINPTRGTHP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IHLHLVSFRV | LDRRPFDIAR | YQESGELSYT | GPAVPPPPSE | KGWKDTIQAH | AGEVLRIAAT |
| 490 | 500 | 510 | |||
| FGPYSGRYVW | HCHILEHEDY | DMMRPMDITD | PHK |