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Magnesium transport protein CorA

 CORA_SALTY              Reviewed;         316 AA.
P0A2R8; P31138;
01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 1.
28-FEB-2018, entry version 86.
RecName: Full=Magnesium transport protein CorA;
Name=corA; OrderedLocusNames=STM3952; ORFNames=STMD1.38;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Salmonella.
NCBI_TaxID=99287;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=8314774;
Smith R.L., Banks J.L., Snavely M.D., Maguire M.E.;
"Sequence and topology of the CorA magnesium transport systems of
Salmonella typhimurium and Escherichia coli. Identification of a new
class of transport protein.";
J. Biol. Chem. 268:14071-14080(1993).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=LT2 / SGSC1412 / ATCC 700720;
PubMed=11677609; DOI=10.1038/35101614;
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
Waterston R., Wilson R.K.;
"Complete genome sequence of Salmonella enterica serovar Typhimurium
LT2.";
Nature 413:852-856(2001).
[3]
FUNCTION, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=LT2;
PubMed=3536881; DOI=10.1128/jb.168.3.1444-1450.1986;
Hmiel S.P., Snavely M.D., Miller C.G., Maguire M.E.;
"Magnesium transport in Salmonella typhimurium: characterization of
magnesium influx and cloning of a transport gene.";
J. Bacteriol. 168:1444-1450(1986).
[4]
FUNCTION.
PubMed=2548998; DOI=10.1128/jb.171.9.4742-4751.1989;
Hmiel S.P., Snavely M.D., Florer J.B., Maguire M.E., Miller C.G.;
"Magnesium transport in Salmonella typhimurium: genetic
characterization and cloning of three magnesium transport loci.";
J. Bacteriol. 171:4742-4751(1989).
[5]
SUBCELLULAR LOCATION.
PubMed=2548999;
Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
"Magnesium transport in Salmonella typhimurium: expression of cloned
genes for three distinct Mg2+ transport systems.";
J. Bacteriol. 171:4752-4760(1989).
[6]
FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=2670893; DOI=10.1128/jb.171.9.4761-4766.1989;
Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
"Magnesium transport in Salmonella typhimurium: (28)Mg2+ transport by
the CorA, MgtA, and MgtB systems.";
J. Bacteriol. 171:4761-4766(1989).
[7]
FUNCTION, AND MUTAGENESIS OF TYR-292 AND MET-299.
PubMed=9786860; DOI=10.1074/jbc.273.44.28663;
Smith R.L., Szegedy M.A., Kucharski L.M., Walker C., Wiet R.M.,
Redpath A., Kaczmarek M.T., Maguire M.E.;
"The CorA Mg2+ transport protein of Salmonella typhimurium.
Mutagenesis of conserved residues in the third membrane domain
identifies a Mg2+ pore.";
J. Biol. Chem. 273:28663-28669(1998).
[8]
FUNCTION, AND MUTAGENESIS OF SER-260; THR-270; SER-274; TYR-276;
GLY-277; MET-278; ASN-279 AND PHE-280.
PubMed=10601252; DOI=10.1074/jbc.274.52.36973;
Szegedy M.A., Maguire M.E.;
"The CorA Mg(2+) transport protein of Salmonella typhimurium.
Mutagenesis of conserved residues in the second membrane domain.";
J. Biol. Chem. 274:36973-36979(1999).
[9]
FUNCTION, INHIBITION BY CATION HEXAAMMINES, AND ENZYME REGULATION.
PubMed=10748031; DOI=10.1074/jbc.M001507200;
Kucharski L.M., Lubbe W.J., Maguire M.E.;
"Cation hexaammines are selective and potent inhibitors of the CorA
magnesium transport system.";
J. Biol. Chem. 275:16767-16773(2000).
[10]
SUBUNIT.
PubMed=15231793; DOI=10.1128/JB.186.14.4605-4612.2004;
Warren M.A., Kucharski L.M., Veenstra A., Shi L., Grulich P.F.,
Maguire M.E.;
"The CorA Mg2+ transporter is a homotetramer.";
J. Bacteriol. 186:4605-4612(2004).
[11]
FUNCTION.
PubMed=15516579; DOI=10.1128/JB.186.22.7653-7658.2004;
Papp K.M., Maguire M.E.;
"The CorA Mg2+ transporter does not transport Fe2+.";
J. Bacteriol. 186:7653-7658(2004).
-!- FUNCTION: Mediates both influx and efflux of magnesium ions
(PubMed:3536881, PubMed:2548998, PubMed:2670893, PubMed:9786860,
PubMed:10601252, PubMed:10748031). Can also mediate cobalt and
nickel uptake, albeit only at extracellular concentrations that
are toxic to the cell (PubMed:3536881, PubMed:2670893). Does not
transport iron (PubMed:15516579). Alternates between open and
closed states. Activated by low cytoplasmic Mg(2+) levels.
Inactive when cytoplasmic Mg(2+) levels are high (By similarity).
{ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:10601252,
ECO:0000269|PubMed:10748031, ECO:0000269|PubMed:15516579,
ECO:0000269|PubMed:2548998, ECO:0000269|PubMed:2670893,
ECO:0000269|PubMed:3536881}.
-!- ENZYME REGULATION: Inhibited by cation hexaammines.
{ECO:0000269|PubMed:10748031}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=15 uM for magnesium ions {ECO:0000269|PubMed:2670893,
ECO:0000269|PubMed:3536881};
KM=30 uM for cobalt ions {ECO:0000269|PubMed:3536881};
KM=300 uM for nickel ions {ECO:0000269|PubMed:3536881};
-!- SUBUNIT: Homopentamer. In the absence of Mg(2+), interactions
between subunits are weakened, and dimers, trimers and tetramers
can be observed in vitro (By similarity). Homotetramer
(PubMed:15231793). {ECO:0000250|UniProtKB:Q9WZ31,
ECO:0000269|PubMed:15231793}.
-!- SUBCELLULAR LOCATION: Cell inner membrane
{ECO:0000269|PubMed:2548999, ECO:0000269|PubMed:8314774,
ECO:0000305|PubMed:10601252}; Multi-pass membrane protein
{ECO:0000269|PubMed:8314774}.
-!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:3536881}.
-!- DOMAIN: The central ion permeation pathway is formed by the first
transmembrane domain from each of the five subunits. Mg(2+)
binding strengthens interactions between subunits and leads to the
formation of a symmetrical homopentamer surrounding a closed ion
permeation pathway. Co(2+) binding also induces a conformation
change. Low Mg(2+) 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. {ECO:0000250|UniProtKB:Q9WZ31}.
-!- MISCELLANEOUS: Is the dominant magnesium transport system under
laboratory growth conditions.
-!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC
1.A.35) family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; L11043; AAA02966.1; -; Unassigned_DNA.
EMBL; AF233324; AAF33440.1; -; Genomic_DNA.
EMBL; AE006468; AAL22796.1; -; Genomic_DNA.
PIR; A47157; A47157.
RefSeq; NP_462837.1; NC_003197.2.
RefSeq; WP_000947139.1; NC_003197.2.
ProteinModelPortal; P0A2R8; -.
SMR; P0A2R8; -.
STRING; 99287.STM3952; -.
TCDB; 1.A.35.1.2; the cora metal ion transporter (mit) family.
PaxDb; P0A2R8; -.
PRIDE; P0A2R8; -.
EnsemblBacteria; AAL22796; AAL22796; STM3952.
GeneID; 1255478; -.
KEGG; stm:STM3952; -.
PATRIC; fig|99287.12.peg.4170; -.
eggNOG; ENOG4107QUT; Bacteria.
eggNOG; COG0598; LUCA.
HOGENOM; HOG000276873; -.
KO; K03284; -.
OMA; RRAVSFM; -.
PhylomeDB; P0A2R8; -.
BioCyc; SENT99287:G1FZD-3991-MONOMER; -.
BRENDA; 3.6.3.2; 2169.
SABIO-RK; P0A2R8; -.
Proteomes; UP000001014; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
GO; GO:0015099; F:nickel cation transmembrane transporter activity; IBA:GO_Central.
GO; GO:0006824; P:cobalt ion transport; IBA:GO_Central.
GO; GO:0015693; P:magnesium ion transport; IBA:GO_Central.
GO; GO:0035444; P:nickel cation transmembrane transport; IBA:GO_Central.
InterPro; IPR004488; Mg/Co-transport_prot_CorA.
InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
Pfam; PF01544; CorA; 1.
TIGRFAMs; TIGR00383; corA; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Cobalt; Complete proteome;
Ion transport; Magnesium; Membrane; Nickel; Reference proteome;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 316 Magnesium transport protein CorA.
/FTId=PRO_0000201532.
TOPO_DOM 1 254 Cytoplasmic. {ECO:0000305}.
TRANSMEM 255 273 Helical. {ECO:0000255}.
TOPO_DOM 274 287 Periplasmic. {ECO:0000305}.
TRANSMEM 288 310 Helical. {ECO:0000255}.
TOPO_DOM 311 316 Cytoplasmic.
{ECO:0000269|PubMed:8314774}.
MOTIF 277 279 Probable selectivity filter.
{ECO:0000250|UniProtKB:Q9WZ31}.
SITE 253 253 Essential for ion permeation.
{ECO:0000250|UniProtKB:Q9WZ31}.
MUTAGEN 260 260 S->V: Reduces magnesium transport by
about 99%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 270 270 T->A,C: Reduces magnesium transport by
about 95%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 274 274 S->A,C: Reduces magnesium transport by
about 95%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 276 276 Y->A,F: Reduces magnesium transport by
about 99%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 277 277 G->A: Reduces magnesium transport by
about 99%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 278 278 M->A,C,I: Reduces magnesium transport by
about 99%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 279 279 N->A,L,Q: Reduces magnesium transport by
about 99%. {ECO:0000269|PubMed:10601252}.
MUTAGEN 280 280 F->A,R,W,Y: Reduces magnesium transport
by about 99%.
{ECO:0000269|PubMed:10601252}.
MUTAGEN 292 292 Y->C,F,I,S: Reduces affinity for
magnesium about 10-fold. Reduces
magnesium transport by about 98%.
{ECO:0000269|PubMed:9786860}.
MUTAGEN 299 299 M->A,C: Reduces affinity for magnesium
50-fold. {ECO:0000269|PubMed:9786860}.
SEQUENCE 316 AA; 36593 MW; B3B5F3161BC93355 CRC64;
MLSAFQLEKN RLTRLEVEES QSLIDAVWVD LVEPDDDERL RVQSELGQSL ATRPELEDIE
ASARFFEDED GLHIHSFFFF EDAEDHAGNS TVAFTIRDGR LFTLRERELP AFRLYRMRAR
SQAMVDGNAY ELLLDLFETK IEQLADEIEN IYSDLEKLSR VIMEGHQGDE YDEALSTLAE
LEDIGWKVRL CLMDTQRALN FLVRKARLPG GQLEQAREIL RDIESLLPHN ESLFQKVNFL
MQAAMGFINI EQNRIIKIFS VVSVVFLPPT LVASSYGMNF EFMPELKWSF GYPGAIIFMI
LAGLAPYLYF KRKNWL


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