CORA_SHIDS
ID CORA_SHIDS Reviewed; 316 AA.
AC Q329Z2;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=SDY_3929;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
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; CP000034; ABB63863.1; -; Genomic_DNA.
DR RefSeq; WP_000947159.1; NC_007606.1.
DR RefSeq; YP_405354.1; NC_007606.1.
DR AlphaFoldDB; Q329Z2; -.
DR SMR; Q329Z2; -.
DR STRING; 300267.SDY_3929; -.
DR EnsemblBacteria; ABB63863; ABB63863; SDY_3929.
DR GeneID; 66672278; -.
DR KEGG; sdy:SDY_3929; -.
DR PATRIC; fig|300267.13.peg.4639; -.
DR HOGENOM; CLU_007127_5_0_6; -.
DR OMA; RQNDDMR; -.
DR Proteomes; UP000002716; 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..316
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000239104"
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
