CORA_SALTI
ID CORA_SALTI Reviewed; 316 AA.
AC P0A2R9; P31138;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=STY3607, t3345;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
CC -!- FUNCTION: Mediates influx of magnesium ions. Can also mediate cobalt
CC and manganese uptake (By similarity). Alternates between open and
CC closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive
CC when cytoplasmic Mg(2+) levels are high (By similarity).
CC {ECO:0000250|UniProtKB:P0ABI4, ECO:0000250|UniProtKB:Q9WZ31}.
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). {ECO:0000250|UniProtKB:Q9WZ31}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0ABI4}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:Q9WZ31}.
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 -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000305}.
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DR EMBL; AL513382; CAD07940.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70873.1; -; Genomic_DNA.
DR RefSeq; NP_457799.1; NC_003198.1.
DR RefSeq; WP_000947139.1; NZ_WSUR01000033.1.
DR AlphaFoldDB; P0A2R9; -.
DR SMR; P0A2R9; -.
DR STRING; 220341.16504485; -.
DR EnsemblBacteria; AAO70873; AAO70873; t3345.
DR KEGG; stt:t3345; -.
DR KEGG; sty:STY3607; -.
DR PATRIC; fig|220341.7.peg.3676; -.
DR eggNOG; COG0598; Bacteria.
DR HOGENOM; CLU_007127_5_0_6; -.
DR OMA; RAVSFMM; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; IEA:InterPro.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
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 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Magnesium; Membrane;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..316
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000201531"
FT TOPO_DOM 1..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..287
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..316
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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"
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
