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Protein

Cobalt/magnesium transport protein CorA

Gene

corA

Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Mediates influx of magnesium ions (PubMed:18276588, PubMed:22722933, PubMed:23781956, PubMed:23112165). 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).1 Publication7 Publications

Enzyme regulationi

Inhibited by cobalt hexaammine.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei288Essential for ion permeation1 Publication1
Sitei294Important for closing the ion permeation pathway in the closed state4 Publications1
Sitei295Threonine that confers selectivity for Co(2+) transport1 Publication1

GO - Molecular functioni

  • cobalt ion binding Source: UniProtKB
  • cobalt ion transmembrane transporter activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • magnesium ion transmembrane transporter activity Source: UniProtKB

GO - Biological processi

  • cobalt ion transport Source: UniProtKB
  • magnesium ion transmembrane transport Source: UniProtKB
  • magnesium ion transport Source: InterPro
  • protein homooligomerization Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ion transport, Transport

Keywords - Ligandi

Cobalt, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAi3.6.3.2. 6331.

Protein family/group databases

TCDBi1.A.35.3.2. the cora metal ion transporter (mit) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Cobalt/magnesium transport protein CorACurated
Gene namesi
Name:corA
Ordered Locus Names:TM_0561
OrganismiThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifieri243274 [NCBI]
Taxonomic lineageiBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga
Proteomesi
  • UP000008183 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 292CytoplasmicCuratedAdd BLAST292
Transmembranei293 – 313Helical6 PublicationsAdd BLAST21
Topological domaini314 – 324ExtracellularCuratedAdd BLAST11
Transmembranei325 – 345Helical6 PublicationsAdd BLAST21
Topological domaini346 – 351CytoplasmicCurated6

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi89D → F or K: Decreases ion transport. 2 Publications1
Mutagenesisi253D → K: Increases protein stability. Decreases ion transport. 2 Publications1
Mutagenesisi280L → A: Decreases ion transport. 1 Publication1
Mutagenesisi288N → L: Abolishes Co(2+) uptake. 2 Publications1
Mutagenesisi291M → A: No effect on ion transport. 1 Publication1
Mutagenesisi294L → A or V: Increases ion transport by suppression of an obstruction in the transmembrane ion permeation pathway. 1 Publication1
Mutagenesisi295T → L: Strongly reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-299. 1 Publication1
Mutagenesisi295T → M: Strongly reduces Co(2+) uptake. 1 Publication1
Mutagenesisi295T → S: No significant decrease of Co(2+) uptake, but abolishes selectivity for Co(2+). 1 Publication1
Mutagenesisi299T → L: Reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-295. 1 Publication1
Mutagenesisi299T → M: No effect on Co(2+) uptake. 1 Publication1
Mutagenesisi299T → S: Abolishes Co(2+) uptake. 1 Publication1
Mutagenesisi303P → A, G or I: Increases ion transport by suppression of a kink in the transmembrane ion permeation pathway. 1 Publication1
Mutagenesisi305T → L: Abolishes Co(2+) uptake. 1 Publication1
Mutagenesisi310I → A: Increases ion transport. 1 Publication1
Mutagenesisi311Y → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi311Y → F: No effect on pentamerization. No effect on ion transport. 1 Publication1
Mutagenesisi312G → A: No effect on pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi312G → F: No effect on pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi313M → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi313M → C, I, L or V: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → A: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → D, E or T: Abolishes pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi314N → Q: No effect on pentamerization. Abolishes ion transport. 1 Publication1
Mutagenesisi315F → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications1
Mutagenesisi315F → W: No effect on pentamerization. Increases ion transport. 1 Publication1
Mutagenesisi318M → A: Impairs pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi318M → I, L or V: No effect on pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → A: Impairs pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → I: No effect on pentamerization. Decreases ion transport. 1 Publication1
Mutagenesisi321L → V: No effect on pentamerization. No effect on ion transport. 1 Publication1
Mutagenesisi327Y → A: Abolishes pentamerization. Strongly decreases ion transport. 2 Publications1
Mutagenesisi327Y → F: No effect on pentamerization. Increases ion transport. 1 Publication1
Mutagenesisi327Y → W: Abolishes pentamerization. Mildly decreases ion transport. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002390491 – 351Cobalt/magnesium transport protein CorAAdd BLAST351

Interactioni

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 Publications

Protein-protein interaction databases

DIPiDIP-59006N.
STRINGi243274.TM0561.

Structurei

Secondary structure

1351
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 7Combined sources3
Beta strandi28 – 35Combined sources8
Beta strandi38 – 45Combined sources8
Helixi47 – 49Combined sources3
Helixi51 – 55Combined sources5
Beta strandi60 – 65Combined sources6
Helixi70 – 80Combined sources11
Helixi84 – 91Combined sources8
Beta strandi98 – 101Combined sources4
Beta strandi103 – 114Combined sources12
Turni117 – 120Combined sources4
Beta strandi123 – 132Combined sources10
Beta strandi135 – 143Combined sources9
Helixi148 – 155Combined sources8
Helixi161 – 163Combined sources3
Helixi166 – 197Combined sources32
Helixi208 – 242Combined sources35
Helixi244 – 272Combined sources29
Helixi275 – 310Combined sources36
Beta strandi311 – 313Combined sources3
Helixi319 – 322Combined sources4
Helixi326 – 344Combined sources19
Turni345 – 348Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BBHX-ray1.85A1-266[»]
2BBJX-ray3.90A/B/D/E/F1-351[»]
2HN2X-ray3.70A/B/C/D/E1-351[»]
2IUBX-ray2.90A/B/C/D/E/F/G/H/I/J1-351[»]
3JCFX-ray3.80A/B/C/D/E1-351[»]
3JCGX-ray7.06A/B/C/D/E1-351[»]
3JCHX-ray7.06A/B/C/D/E1-351[»]
4EEBX-ray3.80A/B/C/D/E26-351[»]
4EEDX-ray3.92A/B/C/D/E26-351[»]
4I0UX-ray2.70A/B/C/D/E/F/G/H/I/J1-351[»]
ProteinModelPortaliQ9WZ31.
SMRiQ9WZ31.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9WZ31.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili178 – 225Sequence analysisAdd BLAST48

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi312 – 314Probable selectivity filter4 Publications3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi346 – 349Poly-Lys4

Domaini

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:23091000, PubMed:16902408, PubMed:16598263, PubMed:16857941, 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).1 Publication7 Publications

Sequence similaritiesi

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105D7N. Bacteria.
COG0598. LUCA.
InParanoidiQ9WZ31.
KOiK03284.
OMAiGENYILY.

Family and domain databases

InterProiIPR004488. Mg/Co-transport_prot_CorA.
IPR002523. MgTranspt_CorA/ZnTranspt_ZntB.
[Graphical view]
PfamiPF01544. CorA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00383. corA. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9WZ31-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:351
Mass (Da):41,446
Last modified:November 1, 1999 - v1
Checksum:i6A845EC612A4A0BA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35646.1.
PIRiH72360.
RefSeqiNP_228371.1. NC_000853.1.
WP_004081315.1. NZ_CP011107.1.

Genome annotation databases

EnsemblBacteriaiAAD35646; AAD35646; TM_0561.
GeneIDi897621.
KEGGitma:TM0561.
PATRICi23936029. VBITheMar51294_0569.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000512 Genomic DNA. Translation: AAD35646.1.
PIRiH72360.
RefSeqiNP_228371.1. NC_000853.1.
WP_004081315.1. NZ_CP011107.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BBHX-ray1.85A1-266[»]
2BBJX-ray3.90A/B/D/E/F1-351[»]
2HN2X-ray3.70A/B/C/D/E1-351[»]
2IUBX-ray2.90A/B/C/D/E/F/G/H/I/J1-351[»]
3JCFX-ray3.80A/B/C/D/E1-351[»]
3JCGX-ray7.06A/B/C/D/E1-351[»]
3JCHX-ray7.06A/B/C/D/E1-351[»]
4EEBX-ray3.80A/B/C/D/E26-351[»]
4EEDX-ray3.92A/B/C/D/E26-351[»]
4I0UX-ray2.70A/B/C/D/E/F/G/H/I/J1-351[»]
ProteinModelPortaliQ9WZ31.
SMRiQ9WZ31.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59006N.
STRINGi243274.TM0561.

Protein family/group databases

TCDBi1.A.35.3.2. the cora metal ion transporter (mit) family.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAD35646; AAD35646; TM_0561.
GeneIDi897621.
KEGGitma:TM0561.
PATRICi23936029. VBITheMar51294_0569.

Phylogenomic databases

eggNOGiENOG4105D7N. Bacteria.
COG0598. LUCA.
InParanoidiQ9WZ31.
KOiK03284.
OMAiGENYILY.

Enzyme and pathway databases

BRENDAi3.6.3.2. 6331.

Miscellaneous databases

EvolutionaryTraceiQ9WZ31.

Family and domain databases

InterProiIPR004488. Mg/Co-transport_prot_CorA.
IPR002523. MgTranspt_CorA/ZnTranspt_ZntB.
[Graphical view]
PfamiPF01544. CorA. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00383. corA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiCORA_THEMA
AccessioniPrimary (citable) accession number: Q9WZ31
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: November 1, 1999
Last modified: November 2, 2016
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.