corA

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

Activity regulationⁱ

Inhibited by cobalt hexaammine.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Siteⁱ	288	Essential for ion permeation1 Publication	1
Siteⁱ	294	Important for closing the ion permeation pathway in the closed state4 Publications	1
Siteⁱ	295	Threonine that confers selectivity for Co(2+) transport1 Publication	1

GO - Molecular functionⁱ

cobalt ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23425532
cobalt ion transmembrane transporter activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23425532
identical protein binding
Source: IntAct
Inferred from physical interactionⁱ
magnesium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 23425532
magnesium ion transmembrane transporter activity
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23112165
- 23781956

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

cobalt ion transport
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23425532
magnesium ion transmembrane transport
Source: UniProtKB
Inferred from mutant phenotypeⁱ
- 23112165
- 23781956
protein homooligomerization
Source: UniProtKB
Inferred from direct assayⁱ
- 23112165
- 23781956

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Ion transport, Transport
Ligand	Cobalt, Magnesium, Metal-binding

Enzyme and pathway databases

BRENDAⁱ	3.6.3.2 6331

BRENDAⁱ

3.6.3.2 6331

Protein family/group databases

TCDBⁱ	1.A.35.3.2 the cora metal ion transporter (mit) family

TCDBⁱ

1.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
Organismⁱ	Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Taxonomic identifierⁱ	243274 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Bacteria › Thermotogae › Thermotogae › Thermotogales › Thermotogaceae › Thermotoga › Thermotoga maritima
Proteomesⁱ	UP000008183 Componentⁱ: Chromosome

Subcellular locationⁱ

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.
1 Publication
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.
; Multi-pass membrane protein
1 Publication
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.
6 Publications
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.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 292	CytoplasmicCuratedAdd BLAST	292
Transmembraneⁱ	293 – 313	Helical6 PublicationsAdd BLAST	21
Topological domainⁱ	314 – 324	ExtracellularCuratedAdd BLAST	11
Transmembraneⁱ	325 – 345	Helical6 PublicationsAdd BLAST	21
Topological domainⁱ	346 – 351	CytoplasmicCurated	6

GO - Cellular componentⁱ

integral component of plasma membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 23112165

View the complete GO annotation on QuickGO ...

Keywords - Cellular componentⁱ

Cell inner membrane, Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	89	D → F or K: Decreases ion transport. 2 Publications	1
Mutagenesisⁱ	253	D → K: Increases protein stability. Decreases ion transport. 2 Publications	1
Mutagenesisⁱ	280	L → A: Decreases ion transport. 1 Publication	1
Mutagenesisⁱ	288	N → L: Abolishes Co(2+) uptake. 2 Publications	1
Mutagenesisⁱ	291	M → A: No effect on ion transport. 1 Publication	1
Mutagenesisⁱ	294	L → A or V: Increases ion transport by suppression of an obstruction in the transmembrane ion permeation pathway. 1 Publication	1
Mutagenesisⁱ	295	T → L: Strongly reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-299. 1 Publication	1
Mutagenesisⁱ	295	T → M: Strongly reduces Co(2+) uptake. 1 Publication	1
Mutagenesisⁱ	295	T → S: No significant decrease of Co(2+) uptake, but abolishes selectivity for Co(2+). 1 Publication	1
Mutagenesisⁱ	299	T → L: Reduces Co(2+) uptake. Abolishes Co(2+) uptake; when associated with L-295. 1 Publication	1
Mutagenesisⁱ	299	T → M: No effect on Co(2+) uptake. 1 Publication	1
Mutagenesisⁱ	299	T → S: Abolishes Co(2+) uptake. 1 Publication	1
Mutagenesisⁱ	303	P → A, G or I: Increases ion transport by suppression of a kink in the transmembrane ion permeation pathway. 1 Publication	1
Mutagenesisⁱ	305	T → L: Abolishes Co(2+) uptake. 1 Publication	1
Mutagenesisⁱ	310	I → A: Increases ion transport. 1 Publication	1
Mutagenesisⁱ	311	Y → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications	1
Mutagenesisⁱ	311	Y → F: No effect on pentamerization. No effect on ion transport. 1 Publication	1
Mutagenesisⁱ	312	G → A: No effect on pentamerization. Abolishes ion transport. 2 Publications	1
Mutagenesisⁱ	312	G → F: No effect on pentamerization. Abolishes ion transport. 1 Publication	1
Mutagenesisⁱ	313	M → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications	1
Mutagenesisⁱ	313	M → C, I, L or V: Abolishes pentamerization. Abolishes ion transport. 1 Publication	1
Mutagenesisⁱ	314	N → A: Abolishes pentamerization. Abolishes ion transport. 1 Publication	1
Mutagenesisⁱ	314	N → D, E or T: Abolishes pentamerization. Abolishes ion transport. 1 Publication	1
Mutagenesisⁱ	314	N → Q: No effect on pentamerization. Abolishes ion transport. 1 Publication	1
Mutagenesisⁱ	315	F → A: Abolishes pentamerization. Abolishes ion transport. 2 Publications	1
Mutagenesisⁱ	315	F → W: No effect on pentamerization. Increases ion transport. 1 Publication	1
Mutagenesisⁱ	318	M → A: Impairs pentamerization. Decreases ion transport. 1 Publication	1
Mutagenesisⁱ	318	M → I, L or V: No effect on pentamerization. Decreases ion transport. 1 Publication	1
Mutagenesisⁱ	321	L → A: Impairs pentamerization. Decreases ion transport. 1 Publication	1
Mutagenesisⁱ	321	L → I: No effect on pentamerization. Decreases ion transport. 1 Publication	1
Mutagenesisⁱ	321	L → V: No effect on pentamerization. No effect on ion transport. 1 Publication	1
Mutagenesisⁱ	327	Y → A: Abolishes pentamerization. Strongly decreases ion transport. 2 Publications	1
Mutagenesisⁱ	327	Y → F: No effect on pentamerization. Increases ion transport. 1 Publication	1
Mutagenesisⁱ	327	Y → W: Abolishes pentamerization. Mildly decreases ion transport. 1 Publication	1

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000239049	1 – 351	Cobalt/magnesium transport protein CorAAdd BLAST		351

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

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
itself		19	EBI-15578365,EBI-15578365

With

Entry

#Exp.

IntAct

Notes

itself

19

EBI-15578365,EBI-15578365

GO - Molecular functionⁱ

identical protein binding
Source: IntAct
Inferred from physical interactionⁱ

View the complete GO annotation on QuickGO ...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-59006N
STRINGⁱ	243274.TM0561

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	5 – 7	Combined sources	3
Beta strandⁱ	28 – 35	Combined sources	8
Beta strandⁱ	38 – 45	Combined sources	8
Helixⁱ	47 – 49	Combined sources	3
Helixⁱ	51 – 55	Combined sources	5
Beta strandⁱ	60 – 65	Combined sources	6
Helixⁱ	70 – 80	Combined sources	11
Helixⁱ	84 – 91	Combined sources	8
Beta strandⁱ	98 – 101	Combined sources	4
Beta strandⁱ	103 – 114	Combined sources	12
Turnⁱ	117 – 120	Combined sources	4
Beta strandⁱ	123 – 132	Combined sources	10
Beta strandⁱ	135 – 143	Combined sources	9
Helixⁱ	148 – 155	Combined sources	8
Helixⁱ	161 – 163	Combined sources	3
Helixⁱ	166 – 197	Combined sources	32
Helixⁱ	208 – 242	Combined sources	35
Helixⁱ	244 – 272	Combined sources	29
Helixⁱ	275 – 310	Combined sources	36
Beta strandⁱ	311 – 313	Combined sources	3
Helixⁱ	319 – 322	Combined sources	4
Helixⁱ	326 – 344	Combined sources	19
Turnⁱ	345 – 348	Combined sources	4

Show more details

3D structure databases

ProteinModelPortalⁱ	Q9WZ31
SMRⁱ	Q9WZ31
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	Q9WZ31

EvolutionaryTraceⁱ

Q9WZ31

Family & Domainsⁱ

Coiled coil

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Coiled coilⁱ	178 – 225	Sequence analysisAdd BLAST		48

Motif

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Motifⁱ	312 – 314	Probable selectivity filter4 Publications		3

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	346 – 349	Poly-Lys		4

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

Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35) family. [View classification]Curated

Keywords - Domainⁱ

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGⁱ	ENOG4105D7N Bacteria COG0598 LUCA
InParanoidⁱ	Q9WZ31
KEGG Orthology (KO) More...KOⁱ	K03284
OMAⁱ	FRDIYDH

Family and domain databases

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
TIGRFAMsⁱ	TIGR00383 corA, 1 hit

Sequenceⁱ

Sequence statusⁱ: Complete.

Q9WZ31-1 [UniParc]FASTA Add 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
PIRⁱ	H72360
NCBI Reference Sequences More...RefSeqⁱ	NP_228371.1, NC_000853.1 WP_004081315.1, NZ_CP011107.1

Genome annotation databases

EnsemblBacteriaⁱ	AAD35646; AAD35646; TM_0561
GeneIDⁱ	897621
KEGGⁱ	tma:TM0561

Protein	Similar proteins		Species	Score	Length	Source
Q9WZ31	Magnesium transport protein CorA		THEMA		351	UniRef100_Q9WZ31
UPI0000DBE12C		THEMT		363

Protein	Similar proteins		Species	Score	Length	Source
Q9WZ31	Magnesium transport protein CorA		THEMA		351	UniRef90_Q9WZ31
Magnesium transport protein CorA (Fragment)		Thermotoga naphthophila		371
Magnesium transport protein CorA		Thermotoga sp. 47_83		351
Magnesium transport protein CorA		THEP1		351
Magnesium transport protein CorA		THENR		351
+8

Protein	Similar proteins		Species	Score	Length	Source
Q9WZ31	Magnesium transport protein CorA		THEMA		351	UniRef50_Q9WZ31
Magnesium transport protein CorA (Fragment)		Thermotoga naphthophila		371
Magnesium transport protein CorA		THESQ		351
Magnesium transport protein CorA		Thermotoga sp. Mc24		351
Magnesium transport protein CorA		Thermotoga sp. 47_83		351
+50

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...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links 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	[»]
ProteinModelPortalⁱ	Q9WZ31
SMRⁱ	Q9WZ31
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

DIPⁱ	DIP-59006N
STRINGⁱ	243274.TM0561

Protein family/group databases

TCDBⁱ	1.A.35.3.2 the cora metal ion transporter (mit) family

TCDBⁱ

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

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

EnsemblBacteriaⁱ	AAD35646; AAD35646; TM_0561
GeneIDⁱ	897621
KEGGⁱ	tma:TM0561

Phylogenomic databases

eggNOGⁱ	ENOG4105D7N Bacteria COG0598 LUCA
InParanoidⁱ	Q9WZ31
KOⁱ	K03284
OMAⁱ	FRDIYDH

Enzyme and pathway databases

BRENDAⁱ	3.6.3.2 6331

BRENDAⁱ

3.6.3.2 6331

Miscellaneous databases

EvolutionaryTraceⁱ	Q9WZ31

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
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	CORA_THEMA
Accessionⁱ	Q9WZ31Primary (citable) accession number: Q9WZ31
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
	Last sequence update:	November 1, 1999
	Last modified:	September 12, 2018
	This is version 119 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Prokaryotic Protein Annotation Program

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UniProtKB - Q9WZ31 (CORA_THEMA)

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Cobalt/magnesium transport protein CorA

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<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

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Enzyme and pathway databases

Protein family/group databases

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Topology

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Keywords - Cellular componenti

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Molecule processing

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Protein-protein interaction databases

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Secondary structure

3D structure databases

Miscellaneous databases

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Coiled coil

Motif

Compositional bias

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Keywords - Domaini

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Genome annotation databases

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Sequence databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ