ID   CORA_ECOL6              Reviewed;         316 AA.
AC   P0ABI5; P27841;
DT   25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=Magnesium transport protein CorA;
GN   Name=corA; OrderedLocusNames=c4737;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83170.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000947159.1; NC_004431.1.
DR   AlphaFoldDB; P0ABI5; -.
DR   SMR; P0ABI5; -.
DR   EnsemblBacteria; AAN83170; AAN83170; c4737.
DR   GeneID; 66672278; -.
DR   KEGG; ecc:c4737; -.
DR   eggNOG; COG0598; Bacteria.
DR   HOGENOM; CLU_007127_5_0_6; -.
DR   OMA; RQNDDMR; -.
DR   Proteomes; UP000001410; 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_0000201529"
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;  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