CORA_BLOFL
ID CORA_BLOFL Reviewed; 314 AA.
AC Q7VRM7;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=Bfl577;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(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 {ECO:0000305}; Multi-pass
CC membrane protein {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; BX248583; CAD83259.1; -; Genomic_DNA.
DR RefSeq; WP_011126835.1; NC_005061.1.
DR AlphaFoldDB; Q7VRM7; -.
DR SMR; Q7VRM7; -.
DR STRING; 203907.Bfl577; -.
DR EnsemblBacteria; CAD83259; CAD83259; Bfl577.
DR KEGG; bfl:Bfl577; -.
DR eggNOG; COG0598; Bacteria.
DR HOGENOM; CLU_007127_5_0_6; -.
DR OMA; RQNDDMR; -.
DR OrthoDB; 822653at2; -.
DR Proteomes; UP000002192; 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 Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..314
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000239089"
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; 36900 MW; 27043EFCAB31BE04 CRC64;
MFNIFQLKNN CLFRMDSQDV ISSINDVIWI DIIQSDDNES HDIQSISEQF KINFFEIKDI
LKNKRFCNSK QGVYIRSFFF SYNEDNQIDN SIVSFIICNN CLYTLRESGF SVFCIYQESL
NNHVLNDGNA YELLLSLFEV KIDDLTDRIE HIYETLERLS FVIMDEQQID GYDSILEDLA
KLESMSWKIH INLLDTERAL QFLVRKVKLP VTQKRHANGI LRGITLLLPY NECIFQKVSF
LTQSVMGLIN IEQNRIIKIF SIVFLPPTLI ASSYGMNFEF MPELKWSFGY PSAIFLMILT
GLAPYLYFKY KKWL