UniProtKB - Q9WZ31 (CORA_THEMA)
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>sp|Q9WZ31|CORA_THEMA Cobalt/magnesium transport protein CorA OS=Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) OX=243274 GN=corA PE=1 SV=1 MEEKRLSAKKGLPPGTLVYTGKYREDFEIEVMNYSIEEFREFKTTDVESVLPFRDSSTPT WINITGIHRTDVVQRVGEFFGIHPLVLEDILNVHQRPKVEFFENYVFIVLKMFTYDKNLH ELESEQVSLILTKNCVLMFQEKIGDVFDPVRERIRYNRGIIRKKRADYLLYSLIDALVDD YFVLLEKIDDEIDVLEEEVLERPEKETVQRTHQLKRNLVELRKTIWPLREVLSSLYRDVP PLIEKETVPYFRDVYDHTIQIADTVETFRDIVSGLLDVYLSSVSNKTNEVMKVLTIIATI FMPLTFIAGIYGMNFEYMPELRWKWGYPVVLAVMGVIAVIMVVYFKKKKWLCommunity curation ()Add a publicationFeedback
Cobalt/magnesium transport protein CorA
corA
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
- Ref.12"Cryo-EM Structures of the magnesium channel CorA reveal symmetry break upon gating."
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.
Cell 164:747-756(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system."
Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.
J. Biol. Chem. 283:11721-11733(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312; MET-313 AND ASN-314. - Ref.3"Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins."
Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P., Eshaghi S.
J. Biol. Chem. 286:16525-16532(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, DOMAIN. - Ref.4"The periplasmic loop provides stability to the open state of the CorA magnesium channel."
Palombo I., Daley D.O., Rapp M.
J. Biol. Chem. 287:27547-27555(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ILE-310; TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.5"Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA."
Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., Cornvik T., Phua T., Eshaghi S.
Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ASN-288, SUBCELLULAR LOCATION. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Manual assertion based on experiment ini
- Ref.2"Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system."
Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.
J. Biol. Chem. 283:11721-11733(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312; MET-313 AND ASN-314.
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei | 288 | Essential for ion permeation1 Publication Manual assertion based on experiment ini
| 1 | |
Sitei | 294 | Important for closing the ion permeation pathway in the closed state4 Publications Manual assertion based on experiment ini
| 1 | |
Sitei | 295 | Threonine that confers selectivity for Co(2+) transport1 Publication Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- cobalt ion binding Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305.
- cobalt ion transmembrane transporter activity Source: UniProtKB
<p>Inferred from Mutant Phenotype</p>
<p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#imp">GO evidence code guide</a></p>
Inferred from mutant phenotypei
- Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305.
- identical protein binding Source: IntAct
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - "Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer."
Dalmas O., Cuello L.G., Jogini V., Cortes D.M., Roux B., Perozo E.
Structure 18:868-878(2010) [PubMed] [Europe PMC] [Abstract] - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN.
- magnesium ion binding Source: UniProtKBInferred from direct assayi
- Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305.
- magnesium ion transmembrane transporter activity Source: UniProtKBInferred from mutant phenotypei
- Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
GO - Biological processi
- cobalt ion transport Source: UniProtKBInferred from mutant phenotypei
- Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305.
- magnesium ion transmembrane transport Source: UniProtKBInferred from mutant phenotypei
- Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
- protein homooligomerization Source: UniProtKBInferred from direct assayi
- Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
Biological process | Ion transport, Transport |
Ligand | Cobalt, Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.6.3.2, 6331 |
Protein family/group databases
Transport Classification Database More...TCDBi | 1.A.35.3.2, the cora metal ion transporter (mit) family |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Cobalt/magnesium transport protein CorACurated |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:corA Ordered Locus Names:TM_0561 |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 243274 [NCBI] |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima |
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Plasma membrane
- Cell inner membrane 10 Publications
Manual assertion inferred by curator fromi
- Ref.2"Probing structure-function relationships and gating mechanisms in the CorA Mg2+ transport system."
Payandeh J., Li C., Ramjeesingh M., Poduch E., Bear C.E., Pai E.F.
J. Biol. Chem. 283:11721-11733(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, ACTIVITY REGULATION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-89; ASP-253; LEU-280; MET-291; LEU-294; PRO-303; GLY-312; MET-313 AND ASN-314. - Ref.3"Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins."
Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P., Eshaghi S.
J. Biol. Chem. 286:16525-16532(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, DOMAIN. - Ref.4"The periplasmic loop provides stability to the open state of the CorA magnesium channel."
Palombo I., Daley D.O., Rapp M.
J. Biol. Chem. 287:27547-27555(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ILE-310; TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.5"Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA."
Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., Cornvik T., Phua T., Eshaghi S.
Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ASN-288, SUBCELLULAR LOCATION. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.7"A structural basis for Mg2+ homeostasis and the CorA translocation cycle."
Payandeh J., Pai E.F.
EMBO J. 25:3762-3773(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MOTIF, DOMAIN, MUTAGENESIS OF ASP-253. - Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.9"Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution."
Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., Nordlund P.
Science 313:354-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305. - Ref.12"Cryo-EM Structures of the magnesium channel CorA reveal symmetry break upon gating."
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.
Cell 164:747-756(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
Manual assertion based on experiment ini
- Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN.
Manual assertion inferred by curator fromi
- Ref.5"Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA."
Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., Cornvik T., Phua T., Eshaghi S.
Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ASN-288, SUBCELLULAR LOCATION.
Manual assertion based on experiment ini
- Ref.7"A structural basis for Mg2+ homeostasis and the CorA translocation cycle."
Payandeh J., Pai E.F.
EMBO J. 25:3762-3773(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MOTIF, DOMAIN, MUTAGENESIS OF ASP-253. - Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.9"Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution."
Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., Nordlund P.
Science 313:354-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305. - Ref.12"Cryo-EM Structures of the magnesium channel CorA reveal symmetry break upon gating."
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.
Cell 164:747-756(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
- Cell inner membrane 10 Publications
Plasma Membrane
- integral component of plasma membrane Source: UniProtKBInferred from direct assayi
- Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN.
- integral component of plasma membrane Source: UniProtKBInferred from direct assayi
Topology
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini | 1 – 292 | CytoplasmicCuratedAdd BLAST | 292 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei | 293 – 313 | Helical6 Publications Manual assertion based on experiment ini
| 21 | |
Topological domaini | 314 – 324 | ExtracellularCuratedAdd BLAST | 11 | |
Transmembranei | 325 – 345 | Helical6 Publications Manual assertion based on experiment ini
| 21 | |
Topological domaini | 346 – 351 | CytoplasmicCurated | 6 |
Keywords - Cellular componenti
Cell inner membrane, Cell membrane, Membrane<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 89 | D → F or K: Decreases ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 253 | D → K: Increases protein stability. Decreases ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 280 | L → A: Decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 288 | N → L: Abolishes Co(2+) uptake. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 291 | M → A: No effect on ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 294 | L → A or V: Increases ion transport by suppression of an obstruction in the transmembrane ion permeation pathway. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 295 | T → L: Strongly reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-299. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 295 | T → M: Strongly reduces Co(2+) uptake. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 295 | T → S: No significant decrease of Co(2+) uptake, but abolishes selectivity for Co(2+). 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 299 | T → L: Reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-295. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 299 | T → M: No effect on Co(2+) uptake. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 299 | T → S: Abolishes Co(2+) uptake. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 303 | P → A, G or I: Increases ion transport by suppression of a kink in the transmembrane ion permeation pathway. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 305 | T → L: Abolishes Co(2+) uptake. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 310 | I → A: Increases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 311 | Y → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 311 | Y → F: No effect on pentamerization. No effect on ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 312 | G → A: No effect on pentamerization. Abolishes ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 312 | G → F: No effect on pentamerization. Abolishes ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 313 | M → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 313 | M → C, I, L or V: Abolishes pentamerization. Abolishes ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 314 | N → A: Abolishes pentamerization. Abolishes ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 314 | N → D, E or T: Abolishes pentamerization. Abolishes ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 314 | N → Q: No effect on pentamerization. Abolishes ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 315 | F → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 315 | F → W: No effect on pentamerization. Increases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 318 | M → A: Impairs pentamerization. Decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 318 | M → I, L or V: No effect on pentamerization. Decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 321 | L → A: Impairs pentamerization. Decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 321 | L → I: No effect on pentamerization. Decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 321 | L → V: No effect on pentamerization. No effect on ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 327 | Y → A: Abolishes pentamerization. Strongly decreases ion transport. 2 Publications Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 327 | Y → F: No effect on pentamerization. Increases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 | |
Mutagenesisi | 327 | Y → W: Abolishes pentamerization. Mildly decreases ion transport. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000239049 | 1 – 351 | Cobalt/magnesium transport protein CorAAdd BLAST | 351 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homopentamer (PubMed:22722933, PubMed:23781956, PubMed:16902408, PubMed:16598263, PubMed:16857941, PubMed:23112165, PubMed:23425532, 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).
8 PublicationsManual assertion based on experiment ini
- Ref.4"The periplasmic loop provides stability to the open state of the CorA magnesium channel."
Palombo I., Daley D.O., Rapp M.
J. Biol. Chem. 287:27547-27555(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF ILE-310; TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.6"Why is the GMN motif conserved in the CorA/Mrs2/Alr1 superfamily of magnesium transport proteins?"
Palombo I., Daley D.O., Rapp M.
Biochemistry 52:4842-4847(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, MUTAGENESIS OF TYR-311; GLY-312; MET-313; ASN-314; PHE-315; MET-318; LEU-321 AND TYR-327. - Ref.7"A structural basis for Mg2+ homeostasis and the CorA translocation cycle."
Payandeh J., Pai E.F.
EMBO J. 25:3762-3773(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MOTIF, DOMAIN, MUTAGENESIS OF ASP-253. - Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.9"Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution."
Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., Nordlund P.
Science 313:354-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305. - Ref.12"Cryo-EM Structures of the magnesium channel CorA reveal symmetry break upon gating."
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.
Cell 164:747-756(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Q9WZ31
With | #Exp. | IntAct |
---|---|---|
itself | 19 | EBI-15578365,EBI-15578365 |
GO - Molecular functioni
- identical protein binding Source: IntActInferred from physical interactioni
- Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - "Structural dynamics of the magnesium-bound conformation of CorA in a lipid bilayer."
Dalmas O., Cuello L.G., Jogini V., Cortes D.M., Roux B., Perozo E.
Structure 18:868-878(2010) [PubMed] [Europe PMC] [Abstract] - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN.
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-59006N |
STRING: functional protein association networks More...STRINGi | 243274.THEMA_01870 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 7 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Beta strandi | 28 – 35 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 38 – 45 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 47 – 49 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 51 – 55 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
Beta strandi | 60 – 65 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
Helixi | 70 – 80 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
Helixi | 84 – 91 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Beta strandi | 98 – 101 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 103 – 114 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
<p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 117 – 120 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Beta strandi | 123 – 132 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
Beta strandi | 135 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
Helixi | 148 – 155 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
Helixi | 161 – 163 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 166 – 197 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 32 | |
Helixi | 208 – 242 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 35 | |
Helixi | 244 – 272 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 29 | |
Helixi | 275 – 310 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 36 | |
Beta strandi | 311 – 313 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
Helixi | 319 – 322 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
Helixi | 326 – 344 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 19 | |
Turni | 345 – 348 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q9WZ31 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q9WZ31 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and domains' section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili | 178 – 225 | Sequence analysisAdd BLAST | 48 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 312 – 314 | Probable selectivity filter4 Publications Manual assertion inferred by curator fromi
| 3 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
<p>This subsection of the 'Family and Domains' section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi | 346 – 349 | Poly-Lys | 4 |
<p>This subsection of the 'Family and domains' section provides general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Manual assertion inferred by curator fromi
- Ref.5"Structural insights into the mechanisms of Mg2+ uptake, transport, and gating by CorA."
Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., Cornvik T., Phua T., Eshaghi S.
Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, MUTAGENESIS OF ASN-288, SUBCELLULAR LOCATION.
Manual assertion based on experiment ini
- Ref.3"Co2+ selectivity of Thermotoga maritima CorA and its inability to regulate Mg2+ homeostasis present a new class of CorA proteins."
Xia Y., Lundbaeck A.K., Sahaf N., Nordlund G., Brzezinski P., Eshaghi S.
J. Biol. Chem. 286:16525-16532(2011) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION IN COBALT TRANSPORT, SUBCELLULAR LOCATION, DOMAIN. - Ref.7"A structural basis for Mg2+ homeostasis and the CorA translocation cycle."
Payandeh J., Pai E.F.
EMBO J. 25:3762-3773(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.70 ANGSTROMS), SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, MOTIF, DOMAIN, MUTAGENESIS OF ASP-253. - Ref.8"Crystal structure of the CorA Mg2+ transporter."
Lunin V.V., Dobrovetsky E., Khutoreskaya G., Zhang R., Joachimiak A., Doyle D.A., Bochkarev A., Maguire M.E., Edwards A.M., Koth C.M.
Nature 440:833-837(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.9"Crystal structure of a divalent metal ion transporter CorA at 2.9 Angstrom resolution."
Eshaghi S., Niegowski D., Kohl A., Molina D.M., Lesley S.A., Nordlund P.
Science 313:354-357(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS), SUBCELLULAR LOCATION, SUBUNIT, TOPOLOGY, DOMAIN, MOTIF. - Ref.10"Structural asymmetry in the magnesium channel CorA points to sequential allosteric regulation."
Pfoh R., Li A., Chakrabarti N., Payandeh J., Pomes R., Pai E.F.
Proc. Natl. Acad. Sci. U.S.A. 109:18809-18814(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.80 ANGSTROMS) OF 26-351 OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN. - Ref.11"Exploring the structure and function of Thermotoga maritima CorA reveals the mechanism of gating and ion selectivity in Co2+/Mg2+ transport."
Nordin N., Guskov A., Phua T., Sahaf N., Xia Y., Lu S., Eshaghi H., Eshaghi S.
Biochem. J. 451:365-374(2013) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY, DOMAIN, MUTAGENESIS OF ASP-89; ASN-288; THR-295; THR-299 AND THR-305. - Ref.12"Cryo-EM Structures of the magnesium channel CorA reveal symmetry break upon gating."
Matthies D., Dalmas O., Borgnia M.J., Dominik P.K., Merk A., Rao P., Reddy B.G., Islam S., Bartesaghi A., Perozo E., Subramaniam S.
Cell 164:747-756(2016) [PubMed] [Europe PMC] [Abstract]Cited for: STRUCTURE BY ELECTRON MICROSCOPY (3.80 ANGSTROMS) OF APOPROTEIN AND IN COMPLEX WITH MAGNESIUM, FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN.
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Keywords - Domaini
Coiled coil, Transmembrane, Transmembrane helixPhylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | COG0598, Bacteria |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | Q9WZ31 |
Identification of Orthologs from Complete Genome Data More...OMAi | MNEIMKV |
Database of Orthologous Groups More...OrthoDBi | 822653at2 |
Family and domain databases
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004488, Mg/Co-transport_prot_CorA IPR002523, MgTranspt_CorA/ZnTranspt_ZntB |
Pfam protein domain database More...Pfami | View protein in Pfam PF01544, CorA, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR00383, corA, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
10 20 30 40 50
MEEKRLSAKK GLPPGTLVYT GKYREDFEIE VMNYSIEEFR EFKTTDVESV
60 70 80 90 100
LPFRDSSTPT WINITGIHRT DVVQRVGEFF GIHPLVLEDI LNVHQRPKVE
110 120 130 140 150
FFENYVFIVL KMFTYDKNLH ELESEQVSLI LTKNCVLMFQ EKIGDVFDPV
160 170 180 190 200
RERIRYNRGI IRKKRADYLL YSLIDALVDD YFVLLEKIDD EIDVLEEEVL
210 220 230 240 250
ERPEKETVQR THQLKRNLVE LRKTIWPLRE VLSSLYRDVP PLIEKETVPY
260 270 280 290 300
FRDVYDHTIQ IADTVETFRD IVSGLLDVYL SSVSNKTNEV MKVLTIIATI
310 320 330 340 350
FMPLTFIAGI YGMNFEYMPE LRWKWGYPVV LAVMGVIAVI MVVYFKKKKW
L
Sequence databases
Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AE000512 Genomic DNA Translation: AAD35646.1 |
Protein sequence database of the Protein Information Resource More...PIRi | H72360 |
NCBI Reference Sequences More...RefSeqi | NP_228371.1, NC_000853.1 WP_004081315.1, NZ_CP011107.1 |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAD35646; AAD35646; TM_0561 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | tma:TM0561 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q9WZ31 | Magnesium transport protein CorA | 351 | UniRef100_Q9WZ31 | |||
+1 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q9WZ31 | Magnesium transport protein CorA | 351 | UniRef90_Q9WZ31 | |||
Magnesium transport protein CorA (Fragment) | 371 | |||||
Magnesium transport protein CorA | 351 | |||||
Magnesium transport protein CorA | 351 | |||||
Magnesium transport protein CorA | 351 | |||||
+10 |
Protein | Similar proteins | Species | Score | Length | Source | |
---|---|---|---|---|---|---|
Q9WZ31 | Magnesium transport protein CorA | 351 | UniRef50_Q9WZ31 | |||
Magnesium transport protein CorA (Fragment) | 371 | |||||
Magnesium transport protein CorA | 351 | |||||
Magnesium transport protein CorA | 351 | |||||
Magnesium transport protein CorA | 351 | |||||
+63 |
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE000512 Genomic DNA Translation: AAD35646.1 |
PIRi | H72360 |
RefSeqi | NP_228371.1, NC_000853.1 WP_004081315.1, NZ_CP011107.1 |
3D structure databases
Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2BBH | X-ray | 1.85 | A | 1-266 | [»] | |
2BBJ | X-ray | 3.90 | A/B/D/E/F | 1-351 | [»] | |
2HN2 | X-ray | 3.70 | A/B/C/D/E | 1-351 | [»] | |
2IUB | X-ray | 2.90 | A/B/C/D/E/F/G/H/I/J | 1-351 | [»] | |
3JCF | X-ray | 3.80 | A/B/C/D/E | 1-351 | [»] | |
3JCG | X-ray | 7.06 | A/B/C/D/E | 1-351 | [»] | |
3JCH | X-ray | 7.06 | A/B/C/D/E | 1-351 | [»] | |
4EEB | X-ray | 3.80 | A/B/C/D/E | 26-351 | [»] | |
4EED | X-ray | 3.92 | A/B/C/D/E | 26-351 | [»] | |
4I0U | X-ray | 2.70 | A/B/C/D/E/F/G/H/I/J | 1-351 | [»] | |
5JRW | X-ray | 3.30 | A/B/C/D/E | 2-351 | [»] | |
5JTG | X-ray | 3.05 | A/B/C/D/E | 2-351 | [»] | |
SMRi | Q9WZ31 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-59006N |
STRINGi | 243274.THEMA_01870 |
Protein family/group databases
TCDBi | 1.A.35.3.2, the cora metal ion transporter (mit) family |
Genome annotation databases
EnsemblBacteriai | AAD35646; AAD35646; TM_0561 |
KEGGi | tma:TM0561 |
Phylogenomic databases
eggNOGi | COG0598, Bacteria |
InParanoidi | Q9WZ31 |
OMAi | MNEIMKV |
OrthoDBi | 822653at2 |
Enzyme and pathway databases
BRENDAi | 3.6.3.2, 6331 |
Miscellaneous databases
EvolutionaryTracei | Q9WZ31 |
Family and domain databases
InterProi | View protein in InterPro IPR004488, Mg/Co-transport_prot_CorA IPR002523, MgTranspt_CorA/ZnTranspt_ZntB |
Pfami | View protein in Pfam PF01544, CorA, 1 hit |
TIGRFAMsi | TIGR00383, corA, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | CORA_THEMA | |
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q9WZ31Primary (citable) accession number: Q9WZ31 | |
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2006 |
Last sequence update: | November 1, 1999 | |
Last modified: | April 7, 2021 | |
This is version 130 of the entry and version 1 of the sequence. See complete history. | ||
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families