P37617
PR
Gene name |
zntA |
Protein name |
Zinc/cadmium/lead-transporting P-type ATPase |
Names |
Pb(II)/Cd(II)/Zn(II)-translocating ATPase, Zn(2+)/Cd(2+)/Pb(2+) export ATPase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b3469 |
EC number |
7.2.2.12: Linked to the hydrolysis of a nucleoside triphosphate |
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
3 structures for P37617
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1MWY | NMR | - | A | 46-118 | PDB |
| 1MWZ | NMR | - | A | 46-118 | PDB |
| AF-P37617-F1 | Predicted | AlphaFoldDB |
No variants for P37617
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P37617 | |||||
No associated diseases with P37617
8 regional properties for P37617
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 194 - 443 | IPR000719 |
| domain | SH2 domain | 79 - 170 | IPR000980 |
| domain | Serine-threonine/tyrosine-protein kinase, catalytic domain | 195 - 438 | IPR001245 |
| domain | SH3 domain | 7 - 69 | IPR001452 |
| active_site | Tyrosine-protein kinase, active site | 307 - 319 | IPR008266 |
| binding_site | Protein kinase, ATP binding site | 200 - 221 | IPR017441 |
| domain | Tyrosine-protein kinase, catalytic domain | 194 - 438 | IPR020635 |
| domain | CSK-like, SH2 domain | 77 - 174 | IPR035027 |
Functions
| Description | ||
|---|---|---|
| EC Number | 7.2.2.12 | Linked to the hydrolysis of a nucleoside triphosphate |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| integral component of plasma membrane | The component of the plasma 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. |
8 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP hydrolysis activity | Catalysis of the reaction: ATP + H2O = ADP + H+ phosphate. ATP hydrolysis is used in some reactions as an energy source, for example to catalyze a reaction or drive transport against a concentration gradient. |
| cadmium ion transmembrane transporter activity | Enables the transfer of cadmium (Cd) ions from one side of a membrane to the other. |
| lead ion transmembrane transporter activity | Enables the transfer of lead (Pb) ions from one side of a membrane to the other. |
| metal ion binding | Binding to a metal ion. |
| P-type cadmium transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Cd2+(in) -> ADP + phosphate + Cd2+(out). |
| P-type zinc transporter activity | Enables the transfer of a solute or solutes from one side of a membrane to the other according to the reaction: ATP + H2O + Zn2+(in) -> ADP + phosphate + Zn2+(out). |
| zinc ion transmembrane transporter activity | Enables the transfer of zinc (Zn) ions from one side of a membrane to the other. |
8 GO annotations of biological process
| Name | Definition |
|---|---|
| cadmium ion transmembrane transport | A process in which a cadmium ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. |
| detoxification of zinc ion | Any process that reduces or removes the toxicity of zinc ion. These include transport of zinc away from sensitive areas and to compartments or complexes whose purpose is sequestration of zinc ion. |
| lead ion transport | The directed movement of lead (Pb) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| response to cadmium ion | 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 a cadmium (Cd) ion stimulus. |
| response to lead ion | 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 a lead ion stimulus. |
| response to zinc ion | 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 a zinc ion stimulus. |
| zinc ion transmembrane transport | A process in which a zinc II ion is transported from one side of a membrane to the other by means of some agent such as a transporter or pore. |
| zinc ion transport | The directed movement of zinc (Zn II) ions into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSTPDNHGKK | APQFAAFKPL | TTVQNANDCC | CDGACSSTPT | LSENVSGTRY | SWKVSGMDCA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ACARKVENAV | RQLAGVNQVQ | VLFATEKLVV | DADNDIRAQV | ESALQKAGYS | LRDEQAAEEP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QASRLKENLP | LITLIVMMAI | SWGLEQFNHP | FGQLAFIATT | LVGLYPIARQ | ALRLIKSGSY |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FAIETLMSVA | AIGALFIGAT | AEAAMVLLLF | LIGERLEGWA | ASRARQGVSA | LMALKPETAT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RLRKGEREEV | AINSLRPGDV | IEVAAGGRLP | ADGKLLSPFA | SFDESALTGE | SIPVERATGD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVPAGATSVD | RLVTLEVLSE | PGASAIDRIL | KLIEEAEERR | APIERFIDRF | SRIYTPAIMA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VALLVTLVPP | LLFAASWQEW | IYKGLTLLLI | GCPCALVIST | PAAITSGLAA | AARRGALIKG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GAALEQLGRV | TQVAFDKTGT | LTVGKPRVTA | IHPATGISES | ELLTLAAAVE | QGATHPLAQA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IVREAQVAEL | AIPTAESQRA | LVGSGIEAQV | NGERVLICAA | GKHPADAFTG | LINELESAGQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| TVVLVVRNDD | VLGVIALQDT | LRADAATAIS | ELNALGVKGV | ILTGDNPRAA | AAIAGELGLE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FKAGLLPEDK | VKAVTELNQH | APLAMVGDGI | NDAPAMKAAA | IGIAMGSGTD | VALETADAAL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| THNHLRGLVQ | MIELARATHA | NIRQNITIAL | GLKGIFLVTT | LLGMTGLWLA | VLADTGATVL |
| 730 | |||||
| VTANALRLLR | RR |