ID   CORA_SHISS              Reviewed;         316 AA.
AC   Q3YVE9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Magnesium transport protein CorA;
GN   Name=corA; OrderedLocusNames=SSON_3991;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ss046;
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA   Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA   Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA   Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT   bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(2005).
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; CP000038; AAZ90513.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q3YVE9; -.
DR   SMR; Q3YVE9; -.
DR   EnsemblBacteria; AAZ90513; AAZ90513; SSON_3991.
DR   KEGG; ssn:SSON_3991; -.
DR   HOGENOM; CLU_007127_5_0_6; -.
DR   OMA; RQNDDMR; -.
DR   Proteomes; UP000002529; 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_0000239105"
FT   TRANSMEM        258..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
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;  36590 MW;  CC3B1B736EE36A53 CRC64;
     MLSAFQLENN RLTRLEVEES QPLVNAVWID LVEPDDDERL RVQSELGQSL ATRPELEDIE
     ASARFFEDDD GLHIHSFFFF EDAEDHAGNS TVAFTIRDGR LFTLRERELP AFRLYRMRAR
     SQSMVDGNAY ELLLDLFETK IEQLADEIEN IYSDLEQLSR VIMEGHQGDE YDEALSTLAE
     LEDIGWKVRL CLMDTQRALN FLVRKARLPG GQLEQAREIL RDIESLLPHN ESLFQKVNFL
     MQAAMGFINI EQNRIIKIFS VVSVVFLPPT LVASSYGMNF EFMPELKWSF GYPGAIIFMI
     LAGLAPYLYF KRKNWL