ID   CORA_BLOPB              Reviewed;         314 AA.
AC   Q491Z9;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Magnesium transport protein CorA;
GN   Name=corA; OrderedLocusNames=BPEN_597;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BPEN;
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(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:Q7VRM7}; 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; CP000016; AAZ41203.1; -; Genomic_DNA.
DR   RefSeq; WP_011283114.1; NC_007292.1.
DR   AlphaFoldDB; Q491Z9; -.
DR   SMR; Q491Z9; -.
DR   STRING; 291272.BPEN_597; -.
DR   EnsemblBacteria; AAZ41203; AAZ41203; BPEN_597.
DR   KEGG; bpn:BPEN_597; -.
DR   eggNOG; COG0598; Bacteria.
DR   HOGENOM; CLU_007127_5_0_6; -.
DR   OMA; RQNDDMR; -.
DR   BioCyc; CBLO291272:BPEN_RS02945-MON; -.
DR   Proteomes; UP000007794; 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..314
FT                   /note="Magnesium transport protein CorA"
FT                   /id="PRO_0000239090"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        288..308
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           275..277
FT                   /note="Probable selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT   SITE            254
FT                   /note="Essential for ion permeation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
SQ   SEQUENCE   314 AA;  36988 MW;  D961659B6F0217C0 CRC64;
     MYNIFQLKNN HLFRINEKDK ISFLNNIIWI DIIDSCGDGH NYIPNILLHQ KIKFFELKDI
     NKTTRFFKDK NGLHIHSFFF SYNSQEQIDN SSVFFTIHNG CLYTSRKKEF PVFCMYQKYL
     HNHLLINGNA YELLLNLFEV KLDDLTNKIE HIYATLETLS SVIMNGQQID EYDHALSDLA
     ILENIGWKIR VNLLDTERAI KFLIRKVKLP VSQQKYANDI LNEITLLLPH NEYVFHQISS
     LTQSAMGFIN IEQNRIIKIF SVIFLPPTLI ASSYGMNFKF MPELQWSFGY PSAIILMILS
     GLAPYIYFKY KNWL