ID   CORA_HAEI8              Reviewed;         315 AA.
AC   Q4QLP6;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Magnesium transport protein CorA;
GN   Name=corA; OrderedLocusNames=NTHI1195;
OS   Haemophilus influenzae (strain 86-028NP).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=281310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=86-028NP;
RX   PubMed=15968074; DOI=10.1128/jb.187.13.4627-4636.2005;
RA   Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B.,
RA   Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O.,
RA   Munson R.S. Jr.;
RT   "Genomic sequence of an otitis media isolate of nontypeable Haemophilus
RT   influenzae: comparative study with H. influenzae serotype d, strain KW20.";
RL   J. Bacteriol. 187:4627-4636(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000057; AAX88051.1; -; Genomic_DNA.
DR   RefSeq; WP_005655990.1; NC_007146.2.
DR   AlphaFoldDB; Q4QLP6; -.
DR   SMR; Q4QLP6; -.
DR   EnsemblBacteria; AAX88051; AAX88051; NTHI1195.
DR   KEGG; hit:NTHI1195; -.
DR   HOGENOM; CLU_007127_5_0_6; -.
DR   OMA; RQNDDMR; -.
DR   OrthoDB; 822653at2; -.
DR   Proteomes; UP000002525; 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..315
FT                   /note="Magnesium transport protein CorA"
FT                   /id="PRO_0000239095"
FT   TRANSMEM        257..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        289..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           276..278
FT                   /note="Probable selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT   SITE            252
FT                   /note="Essential for ion permeation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
SQ   SEQUENCE   315 AA;  36576 MW;  E6601A298D6C4DCF CRC64;
     MINAFAINDS RLVRIDEDQT DLNTAIWLDL LEPTGEEREI LQEGLGQSLA SFLELEDIEA
     SARFFEDEDG LHLHSFFYCE DEDNYADLAS VAFTIRDGRL FTLRDRELPA FRLYRMRSRS
     QRLLECNSYE VLLDLFETKI EQLADVIENI YADLEELSRV ILNGKQDEAF DEALNTLTEQ
     EDTSSKVRLC LMDTQRALGF LVRKTRLPTN QLEQAREILR DIESLQPHNE SLFQKVNFLM
     QAAMGYINIE QNKIMKFFSV VSVMFLPATL VASTYGMNFD FMPELHFKYG YPMAIGLMIA
     AALTPYIYFR RKGWL