Q9WZ31 · CORA_THEMA
- ProteinCobalt/magnesium transport protein CorA
- GenecorA
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids351 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Mediates influx of magnesium ions (PubMed:18276588, PubMed:22722933, PubMed:23112165, PubMed:23781956).
Mediates Co2+ uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532).
Has high selectivity for Co2+ (PubMed:21454699, PubMed:23425532).
Alternates between open and closed states. Activated by low cytoplasmic Mg2+ levels. Inactive when cytoplasmic Mg2+ levels are high (PubMed:23112165, PubMed:23425532, PubMed:26871634).
Mediates Co2+ uptake (PubMed:21454699, PubMed:23091000, PubMed:23425532).
Has high selectivity for Co2+ (PubMed:21454699, PubMed:23425532).
Alternates between open and closed states. Activated by low cytoplasmic Mg2+ levels. Inactive when cytoplasmic Mg2+ levels are high (PubMed:23112165, PubMed:23425532, PubMed:26871634).
Catalytic activity
- Mg2+(in) = Mg2+(out)
- Co2+(in) = Co2+(out)
Activity regulation
Inhibited by cobalt hexaammine.
Features
Showing features for site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 288 | Essential for ion permeation | ||||
Sequence: N | ||||||
Site | 294 | Important for closing the ion permeation pathway in the closed state | ||||
Sequence: L | ||||||
Site | 295 | Threonine that confers selectivity for Co2+ transport | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | cobalt ion binding | |
Molecular Function | cobalt ion transmembrane transporter activity | |
Molecular Function | identical protein binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | magnesium ion transmembrane transporter activity | |
Biological Process | cobalt ion transport | |
Biological Process | magnesium ion transmembrane transport | |
Biological Process | protein homooligomerization |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCobalt/magnesium transport protein CorA
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermotogota > Thermotogae > Thermotogales > Thermotogaceae > Thermotoga
Accessions
- Primary accessionQ9WZ31
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-292 | Cytoplasmic | ||||
Sequence: MEEKRLSAKKGLPPGTLVYTGKYREDFEIEVMNYSIEEFREFKTTDVESVLPFRDSSTPTWINITGIHRTDVVQRVGEFFGIHPLVLEDILNVHQRPKVEFFENYVFIVLKMFTYDKNLHELESEQVSLILTKNCVLMFQEKIGDVFDPVRERIRYNRGIIRKKRADYLLYSLIDALVDDYFVLLEKIDDEIDVLEEEVLERPEKETVQRTHQLKRNLVELRKTIWPLREVLSSLYRDVPPLIEKETVPYFRDVYDHTIQIADTVETFRDIVSGLLDVYLSSVSNKTNEVMK | ||||||
Transmembrane | 293-313 | Helical | ||||
Sequence: VLTIIATIFMPLTFIAGIYGM | ||||||
Topological domain | 314-324 | Extracellular | ||||
Sequence: NFEYMPELRWK | ||||||
Transmembrane | 325-345 | Helical | ||||
Sequence: WGYPVVLAVMGVIAVIMVVYF | ||||||
Topological domain | 346-351 | Cytoplasmic | ||||
Sequence: KKKKWL |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 89 | Decreases ion transport. | ||||
Sequence: D → F or K | ||||||
Mutagenesis | 253 | Increases protein stability. Decreases ion transport. | ||||
Sequence: D → K | ||||||
Mutagenesis | 280 | Decreases ion transport. | ||||
Sequence: L → A | ||||||
Mutagenesis | 288 | Abolishes Co2+ uptake. | ||||
Sequence: N → L | ||||||
Mutagenesis | 291 | No effect on ion transport. | ||||
Sequence: M → A | ||||||
Mutagenesis | 294 | Increases ion transport by suppression of an obstruction in the transmembrane ion permeation pathway. | ||||
Sequence: L → A or V | ||||||
Mutagenesis | 295 | Strongly reduces Co2+ uptake. Abolishes Co2+ uptake; when associated with L-299. | ||||
Sequence: T → L | ||||||
Mutagenesis | 295 | Strongly reduces Co2+ uptake. | ||||
Sequence: T → M | ||||||
Mutagenesis | 295 | No significant decrease of Co2+ uptake, but abolishes selectivity for Co2+. | ||||
Sequence: T → S | ||||||
Mutagenesis | 299 | Reduces Co2+ uptake. Abolishes Co2+ uptake; when associated with L-295. | ||||
Sequence: T → L | ||||||
Mutagenesis | 299 | No effect on Co2+ uptake. | ||||
Sequence: T → M | ||||||
Mutagenesis | 299 | Abolishes Co2+ uptake. | ||||
Sequence: T → S | ||||||
Mutagenesis | 303 | Increases ion transport by suppression of a kink in the transmembrane ion permeation pathway. | ||||
Sequence: P → A, G, or I | ||||||
Mutagenesis | 305 | Abolishes Co2+ uptake. | ||||
Sequence: T → L | ||||||
Mutagenesis | 310 | Increases ion transport. | ||||
Sequence: I → A | ||||||
Mutagenesis | 311 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 311 | No effect on pentamerization. No effect on ion transport. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 312 | No effect on pentamerization. Abolishes ion transport. | ||||
Sequence: G → A | ||||||
Mutagenesis | 312 | No effect on pentamerization. Abolishes ion transport. | ||||
Sequence: G → F | ||||||
Mutagenesis | 313 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: M → A | ||||||
Mutagenesis | 313 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: M → C, I, L, or V | ||||||
Mutagenesis | 314 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: N → A | ||||||
Mutagenesis | 314 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: N → D, E, or T | ||||||
Mutagenesis | 314 | No effect on pentamerization. Abolishes ion transport. | ||||
Sequence: N → Q | ||||||
Mutagenesis | 315 | Abolishes pentamerization. Abolishes ion transport. | ||||
Sequence: F → A | ||||||
Mutagenesis | 315 | No effect on pentamerization. Increases ion transport. | ||||
Sequence: F → W | ||||||
Mutagenesis | 318 | Impairs pentamerization. Decreases ion transport. | ||||
Sequence: M → A | ||||||
Mutagenesis | 318 | No effect on pentamerization. Decreases ion transport. | ||||
Sequence: M → I, L, or V | ||||||
Mutagenesis | 321 | Impairs pentamerization. Decreases ion transport. | ||||
Sequence: L → A | ||||||
Mutagenesis | 321 | No effect on pentamerization. Decreases ion transport. | ||||
Sequence: L → I | ||||||
Mutagenesis | 321 | No effect on pentamerization. No effect on ion transport. | ||||
Sequence: L → V | ||||||
Mutagenesis | 327 | Abolishes pentamerization. Strongly decreases ion transport. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 327 | No effect on pentamerization. Increases ion transport. | ||||
Sequence: Y → F | ||||||
Mutagenesis | 327 | Abolishes pentamerization. Mildly decreases ion transport. | ||||
Sequence: Y → W |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000239049 | 1-351 | Cobalt/magnesium transport protein CorA | |||
Sequence: MEEKRLSAKKGLPPGTLVYTGKYREDFEIEVMNYSIEEFREFKTTDVESVLPFRDSSTPTWINITGIHRTDVVQRVGEFFGIHPLVLEDILNVHQRPKVEFFENYVFIVLKMFTYDKNLHELESEQVSLILTKNCVLMFQEKIGDVFDPVRERIRYNRGIIRKKRADYLLYSLIDALVDDYFVLLEKIDDEIDVLEEEVLERPEKETVQRTHQLKRNLVELRKTIWPLREVLSSLYRDVPPLIEKETVPYFRDVYDHTIQIADTVETFRDIVSGLLDVYLSSVSNKTNEVMKVLTIIATIFMPLTFIAGIYGMNFEYMPELRWKWGYPVVLAVMGVIAVIMVVYFKKKKWL |
Proteomic databases
Interaction
Subunit
Homopentamer (PubMed:16598263, PubMed:16857941, PubMed:16902408, PubMed:22722933, PubMed:23112165, PubMed:23425532, PubMed:23781956, PubMed:26871634).
In the absence of Mg2+, interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (PubMed:22722933, PubMed:26871634).
In the absence of Mg2+, interactions between subunits are weakened, and dimers, trimers and tetramers can be observed in vitro (PubMed:22722933, PubMed:26871634).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9WZ31 | corA Q9WZ31 | 19 | EBI-15578365, EBI-15578365 |
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for coiled coil, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Coiled coil | 178-225 | |||||
Sequence: VDDYFVLLEKIDDEIDVLEEEVLERPEKETVQRTHQLKRNLVELRKTI | ||||||
Motif | 312-314 | Probable selectivity filter | ||||
Sequence: GMN |
Domain
The central ion permeation pathway is formed by the first transmembrane domain from each of the five subunits. Mg2+ binding strengthens interactions between subunits and leads to the formation of a symmetrical homopentamer surrounding a closed ion permeation pathway (PubMed:16598263, PubMed:16857941, PubMed:16902408, PubMed:23091000, PubMed:23112165, PubMed:23425532, PubMed:26871634).
Co2+ binding also induces a conformation change (PubMed:21454699).
Low Mg2+ concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex (PubMed:23112165, PubMed:26871634).
Co2+ binding also induces a conformation change (PubMed:21454699).
Low Mg2+ concentrations trigger both a conformation change within each subunit and a loosening of the interactions between subunits. This results in an open ion conduction pathway. In addition, this results in a less symmetrical shape of the whole complex (PubMed:23112165, PubMed:26871634).
Sequence similarities
Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length351
- Mass (Da)41,446
- Last updated1999-11-01 v1
- Checksum6A845EC612A4A0BA
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE000512 EMBL· GenBank· DDBJ | AAD35646.1 EMBL· GenBank· DDBJ | Genomic DNA |