A0A378K7V6
Gene name |
lapB (NCTC12000_01543) |
Protein name |
Lipopolysaccharide assembly protein B |
Names |
|
Species |
Legionella pneumophila |
KEGG Pathway |
|
EC number |
|
Protein Class |
TPR REPEAT-CONTAINING PROTEIN PA4667 (PTHR45586) |
Descriptions
LapB is an amino peptidase that catalyzed the removal of a wide range of N-terminal amino acid residues from peptides and proteins. Autoinhibition of LapB is mediated by the N-terminal protease-associated (PA) domain which covers the active site of the peptidase domain, inhibiting catalytic activity. This autoinhibition can be alleviated by conformational changes induced by organic solvents, significantly increasing enzyme activity.
Autoinhibitory domains (AIDs)
Target domain |
262-345 (Active site of the peptidase domain) |
Relief mechanism |
Partner binding |
Assay |
Deletion assay, Structural analysis |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A0A378K7V6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0A378K7V6-F1 | Predicted | AlphaFoldDB |
No variants for A0A378K7V6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0A378K7V6 | |||||
No associated diseases with A0A378K7V6
6 regional properties for A0A378K7V6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| repeat | Tetratricopeptide repeat | 35 - 68 | IPR019734-1 |
| repeat | Tetratricopeptide repeat | 69 - 102 | IPR019734-2 |
| repeat | Tetratricopeptide repeat | 107 - 140 | IPR019734-3 |
| repeat | Tetratricopeptide repeat | 181 - 214 | IPR019734-4 |
| repeat | Tetratricopeptide repeat | 215 - 248 | IPR019734-5 |
| domain | LapB, rubredoxin metal binding domain | 355 - 382 | IPR041166 |
Functions
| Description | ||
|---|---|---|
| EC Number | ||
| Subcellular Localization |
|
|
| PANTHER Family | PTHR45586 | TPR REPEAT-CONTAINING PROTEIN PA4667 |
| PANTHER Subfamily | PTHR45586:SF17 | LIPOPOLYSACCHARIDE ASSEMBLY PROTEIN B |
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasmic side of plasma membrane | The leaflet the plasma membrane that faces the cytoplasm and any proteins embedded or anchored in it or attached to its surface. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| iron ion binding | Binding to an iron (Fe) ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| lipopolysaccharide metabolic process | The chemical reactions and pathways involving lipopolysaccharides, a group of related, structurally complex components of the outer membrane of Gram-negative bacteria. Lipopolysaccharides consist three covalently linked regions, lipid A, core oligosaccharide, and an O side chain. Lipid A is responsible for the toxicity of the lipopolysaccharide. |
| regulation of lipid biosynthetic process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of lipids. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MINLWPLLLP | AAAWSGWWLA | SRSNSNKDAH | VHNRLSREYV | VGLNYLLNEQ | SDKAVDVFIK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLEVDSDTVE | THLALGSLFR | RRGEVDRAIR | IHQNLIARPQ | LSIQQRKEAL | MALGQDYMSA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GVFDRAERIF | LEVVELGGSR | DTSSLQGLLA | IYQQEKAWEK | ALDIIKKLEI | STGASFHNQA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AHYYCEMASQ | ALKINAMDRA | IYCIKQAMNV | DPESVRASLM | NATIEIKEGR | YKQAIRSLKR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VPQQDAEFLT | EIIEPLVLCH | KELDSMPDCI | HYLEQTLEKH | PRASVIFVIA | DYLRQNKGMD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IAIDFVADNL | SKHPSIRGLN | RLIYWHLESA | HGKVREKLQM | LYDITSKFLD | NKPIYRCGHC |
| 370 | 380 | ||||
| GFGGKHLHWH | CPSCKQWGRM | KPIHGLEGD |