C0ZL89
Gene name |
lysX (RER_00710) |
Protein name |
Lysylphosphatidylglycerol biosynthesis bifunctional protein LysX |
Names |
|
Species |
Rhodococcus erythropolis (strain PR4 / NBRC 100887) |
KEGG Pathway |
rer:RER_00710 |
EC number |
2.3.2.3: Aminoacyltransferases |
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 C0ZL89
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C0ZL89-F1 | Predicted | AlphaFoldDB |
No variants for C0ZL89
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C0ZL89 | |||||
No associated diseases with C0ZL89
11 regional properties for C0ZL89
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 759 - 1099 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 664 - 739 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 783 - 1102 | IPR006195 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 795 - 805 | IPR018149-1 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 811 - 827 | IPR018149-2 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 840 - 853 | IPR018149-3 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 858 - 875 | IPR018149-4 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 986 - 1002 | IPR018149-5 |
| domain | Phosphatidylglycerol lysyltransferase, C-terminal | 246 - 548 | IPR024320 |
| domain | Lysyl-tRNA synthetase, N-terminal transmembrane region | 19 - 227 | IPR031553 |
| domain | Lysine-tRNA ligase, class II, N-terminal | 663 - 769 | IPR044136 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.3.2.3 | Aminoacyltransferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 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). |
| lysine-tRNA ligase activity | Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). |
| lysyltransferase activity | Catalysis of the reaction: L-lysyl-tRNA + phosphatidylglycerol = tRNA + 3-phosphatidyl-1'-(3'-O-L-lysyl)glycerol. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| lipid metabolic process | The chemical reactions and pathways involving lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. Includes fatty acids; neutral fats, other fatty-acid esters, and soaps; long-chain (fatty) alcohols and waxes; sphingoids and other long-chain bases; glycolipids, phospholipids and sphingolipids; and carotenes, polyprenols, sterols, terpenes and other isoprenoids. |
| lysyl-tRNA aminoacylation | The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA. |
| 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 |
| MESPPENPRQ | ARRFRKGRFS | QVPHISGLIL | GVFSVLVFLW | SISPVLRHIL | RVPREYIDSY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| YFDAPDTSLS | WALVVALLAA | ALASRKRIAW | WLLTIYLALI | TLTNIASTIV | DKNPNNAVAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VVLLVVIGIL | IAARPEFYTR | VRRGAGWKAL | GVLIGGMAVA | TVIGWGLVEL | FPGDLPQNQR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FLWALNRVTA | AASVDNEVFD | GHPRVFVNTV | LGLLGAIALL | AAVMTLFRAQ | RSNNALTGND |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ESAIRGLIQN | FGADDSLAYF | ATRRDKAVIF | APSGKAAITY | RVEIGVCLAS | GDPIGDPEAW |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PHAIEAWQDL | ASQYGWATAV | MGASETGATA | YKKAGLSVLQ | LGDEAILRTR | EFNLNGRDMR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PVRQAVTRVR | RHGVTVRMRR | HRDIPPEDMA | AVIIRADDWR | DTDTERGFSM | ALGRLGDHLD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GDCLLVEAVM | GEGTEDESVV | GMLSLVPWGP | NGVSLDLMRR | KPTAPNGVVE | LMVSELATRS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DEIGVVRVSL | NFAVFRSVFE | EGSRIGAGPI | LRIWRSVLVF | FSRWWQLEAL | YRSNVKYQPD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| WEPRFLCFED | NRELPRVGFA | SAIAEGFVVL | PSFGRKSSQV | VKHTGTHAAV | PAALVTSEGL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| HADGSPPDSA | PSFTTNGPRR | PEQVRVRMNK | LAQLADEGIA | AYPVAYPPTH | TIAAAAKSPE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| GTRVRIAGRL | LRVRDYGGVV | FTDVRDWSGD | IQVLVDQDNV | GREKLAEFAA | EFDLGDLIEV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SGTIGRSRKG | ELSLIAVEWR | MNGKCLHPLP | DKWKGLSDPE | TRVRQRYLDI | ALNPKARELL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EARSAVVKSL | RDSLGGRGYL | EVETPILQQV | HGGANAAPFL | THINAYNLDL | YLRIAPELYL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KRLCVAGMEK | VFEIGRVFRN | EGVDFKHNPE | FTILEAYEAH | SDYEGMMRMC | RELIQAAAVA |
| 910 | 920 | 930 | 940 | 950 | 960 |
| AFGREIIMRP | GPDGELVEVD | ISGEWPVKTM | HGAVAEKLGV | DVSPETSLED | LQKLCDANEI |
| 970 | 980 | 990 | 1000 | 1010 | 1020 |
| PYQSSWDTGA | IAQEMYEHLV | EDYTEFPTFY | TNFPTSMSPL | TRPHRSIPGV | AEKWDLVAWG |
| 1030 | 1040 | 1050 | 1060 | 1070 | 1080 |
| VELGTAYSEL | TDPVDQRNRL | TEQSMLAAGG | DPEAMELDED | FLQALEHAMP | PTGGLGMGVD |
| 1090 | 1100 | ||||
| RIVMLITGGS | IRETLAFPLA | KPRQ |