CORA_SALTY
ID CORA_SALTY Reviewed; 316 AA.
AC P0A2R8; P31138;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=STM3952; ORFNames=STMD1.38;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=8314774; DOI=10.1016/s0021-9258(19)85210-9;
RA Smith R.L., Banks J.L., Snavely M.D., Maguire M.E.;
RT "Sequence and topology of the CorA magnesium transport systems of
RT Salmonella typhimurium and Escherichia coli. Identification of a new class
RT of transport protein.";
RL J. Biol. Chem. 268:14071-14080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP FUNCTION, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=LT2;
RX PubMed=3536881; DOI=10.1128/jb.168.3.1444-1450.1986;
RA Hmiel S.P., Snavely M.D., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: characterization of
RT magnesium influx and cloning of a transport gene.";
RL J. Bacteriol. 168:1444-1450(1986).
RN [4]
RP FUNCTION.
RX PubMed=2548998; DOI=10.1128/jb.171.9.4742-4751.1989;
RA Hmiel S.P., Snavely M.D., Florer J.B., Maguire M.E., Miller C.G.;
RT "Magnesium transport in Salmonella typhimurium: genetic characterization
RT and cloning of three magnesium transport loci.";
RL J. Bacteriol. 171:4742-4751(1989).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=2548999; DOI=10.1128/jb.171.9.4752-4760.1989;
RA Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: expression of cloned genes
RT for three distinct Mg2+ transport systems.";
RL J. Bacteriol. 171:4752-4760(1989).
RN [6]
RP FUNCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=2670893; DOI=10.1128/jb.171.9.4761-4766.1989;
RA Snavely M.D., Florer J.B., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: (28)Mg2+ transport by the
RT CorA, MgtA, and MgtB systems.";
RL J. Bacteriol. 171:4761-4766(1989).
RN [7]
RP FUNCTION, AND MUTAGENESIS OF TYR-292 AND MET-299.
RX PubMed=9786860; DOI=10.1074/jbc.273.44.28663;
RA Smith R.L., Szegedy M.A., Kucharski L.M., Walker C., Wiet R.M., Redpath A.,
RA Kaczmarek M.T., Maguire M.E.;
RT "The CorA Mg2+ transport protein of Salmonella typhimurium. Mutagenesis of
RT conserved residues in the third membrane domain identifies a Mg2+ pore.";
RL J. Biol. Chem. 273:28663-28669(1998).
RN [8]
RP FUNCTION, AND MUTAGENESIS OF SER-260; THR-270; SER-274; TYR-276; GLY-277;
RP MET-278; ASN-279 AND PHE-280.
RX PubMed=10601252; DOI=10.1074/jbc.274.52.36973;
RA Szegedy M.A., Maguire M.E.;
RT "The CorA Mg(2+) transport protein of Salmonella typhimurium. Mutagenesis
RT of conserved residues in the second membrane domain.";
RL J. Biol. Chem. 274:36973-36979(1999).
RN [9]
RP FUNCTION, INHIBITION BY CATION HEXAAMMINES, AND ACTIVITY REGULATION.
RX PubMed=10748031; DOI=10.1074/jbc.m001507200;
RA Kucharski L.M., Lubbe W.J., Maguire M.E.;
RT "Cation hexaammines are selective and potent inhibitors of the CorA
RT magnesium transport system.";
RL J. Biol. Chem. 275:16767-16773(2000).
RN [10]
RP SUBUNIT.
RX PubMed=15231793; DOI=10.1128/jb.186.14.4605-4612.2004;
RA Warren M.A., Kucharski L.M., Veenstra A., Shi L., Grulich P.F.,
RA Maguire M.E.;
RT "The CorA Mg2+ transporter is a homotetramer.";
RL J. Bacteriol. 186:4605-4612(2004).
RN [11]
RP FUNCTION.
RX PubMed=15516579; DOI=10.1128/jb.186.22.7653-7658.2004;
RA Papp K.M., Maguire M.E.;
RT "The CorA Mg2+ transporter does not transport Fe2+.";
RL J. Bacteriol. 186:7653-7658(2004).
CC -!- FUNCTION: Mediates both influx and efflux of magnesium ions
CC (PubMed:3536881, PubMed:2548998, PubMed:2670893, PubMed:9786860,
CC PubMed:10601252, PubMed:10748031). Can also mediate cobalt and nickel
CC uptake, albeit only at extracellular concentrations that are toxic to
CC the cell (PubMed:3536881, PubMed:2670893). Does not transport iron
CC (PubMed:15516579). Alternates between open and closed states. Activated
CC by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+)
CC levels are high (By similarity). {ECO:0000250|UniProtKB:Q9WZ31,
CC ECO:0000269|PubMed:10601252, ECO:0000269|PubMed:10748031,
CC ECO:0000269|PubMed:15516579, ECO:0000269|PubMed:2548998,
CC ECO:0000269|PubMed:2670893, ECO:0000269|PubMed:3536881}.
CC -!- ACTIVITY REGULATION: Inhibited by cation hexaammines.
CC {ECO:0000269|PubMed:10748031}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=15 uM for magnesium ions {ECO:0000269|PubMed:2670893,
CC ECO:0000269|PubMed:3536881};
CC KM=30 uM for cobalt ions {ECO:0000269|PubMed:3536881};
CC KM=300 uM for nickel ions {ECO:0000269|PubMed:3536881};
CC -!- SUBUNIT: Homopentamer. In the absence of Mg(2+), interactions between
CC subunits are weakened, and dimers, trimers and tetramers can be
CC observed in vitro (By similarity). Homotetramer (PubMed:15231793).
CC {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:15231793}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:2548999,
CC ECO:0000269|PubMed:8314774, ECO:0000305|PubMed:10601252}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:8314774}.
CC -!- INDUCTION: Constitutively expressed. {ECO:0000269|PubMed:3536881}.
CC -!- DOMAIN: The central ion permeation pathway is formed by the first
CC transmembrane domain from each of the five subunits. Mg(2+) binding
CC strengthens interactions between subunits and leads to the formation of
CC a symmetrical homopentamer surrounding a closed ion permeation pathway.
CC Co(2+) binding also induces a conformation change. Low Mg(2+)
CC concentrations trigger both a conformation change within each subunit
CC and a loosening of the interactions between subunits. This results in
CC an open ion conduction pathway. In addition, this results in a less
CC symmetrical shape of the whole complex. {ECO:0000250|UniProtKB:Q9WZ31}.
CC -!- MISCELLANEOUS: Is the dominant magnesium transport system under
CC laboratory growth conditions.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
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DR EMBL; L11043; AAA02966.1; -; Unassigned_DNA.
DR EMBL; AF233324; AAF33440.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL22796.1; -; Genomic_DNA.
DR PIR; A47157; A47157.
DR RefSeq; NP_462837.1; NC_003197.2.
DR RefSeq; WP_000947139.1; NC_003197.2.
DR AlphaFoldDB; P0A2R8; -.
DR SMR; P0A2R8; -.
DR STRING; 99287.STM3952; -.
DR TCDB; 1.A.35.1.2; the cora metal ion transporter (mit) family.
DR PaxDb; P0A2R8; -.
DR PRIDE; P0A2R8; -.
DR EnsemblBacteria; AAL22796; AAL22796; STM3952.
DR GeneID; 1255478; -.
DR KEGG; stm:STM3952; -.
DR PATRIC; fig|99287.12.peg.4170; -.
DR HOGENOM; CLU_007127_5_0_6; -.
DR OMA; RAVSFMM; -.
DR PhylomeDB; P0A2R8; -.
DR BioCyc; SENT99287:STM3952-MON; -.
DR BRENDA; 7.2.2.14; 2169.
DR SABIO-RK; P0A2R8; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IBA:GO_Central.
DR InterPro; IPR045861; CorA_cytoplasmic_dom.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR004488; Mg/Co-transport_prot_CorA.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR Pfam; PF01544; CorA; 1.
DR SUPFAM; SSF143865; SSF143865; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
DR TIGRFAMs; TIGR00383; corA; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Cobalt; Ion transport; Magnesium;
KW Membrane; Nickel; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..316
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000201532"
FT TOPO_DOM 1..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..287
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:8314774"
FT MOTIF 277..279
FT /note="Probable selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT SITE 253
FT /note="Essential for ion permeation"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT MUTAGEN 260
FT /note="S->V: Reduces magnesium transport by about 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 270
FT /note="T->A,C: Reduces magnesium transport by about 95%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 274
FT /note="S->A,C: Reduces magnesium transport by about 95%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 276
FT /note="Y->A,F: Reduces magnesium transport by about 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 277
FT /note="G->A: Reduces magnesium transport by about 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 278
FT /note="M->A,C,I: Reduces magnesium transport by about 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 279
FT /note="N->A,L,Q: Reduces magnesium transport by about 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 280
FT /note="F->A,R,W,Y: Reduces magnesium transport by about
FT 99%."
FT /evidence="ECO:0000269|PubMed:10601252"
FT MUTAGEN 292
FT /note="Y->C,F,I,S: Reduces affinity for magnesium about 10-
FT fold. Reduces magnesium transport by about 98%."
FT /evidence="ECO:0000269|PubMed:9786860"
FT MUTAGEN 299
FT /note="M->A,C: Reduces affinity for magnesium 50-fold."
FT /evidence="ECO:0000269|PubMed:9786860"
SQ 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
