CORA_METJA
ID CORA_METJA Reviewed; 317 AA.
AC Q58439;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Cobalt/magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=MJ1033;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9573171; DOI=10.1128/jb.180.10.2788-2791.1998;
RA Smith R.L., Gottlieb E., Kucharski L.M., Maguire M.E.;
RT "Functional similarity between archaeal and bacterial CorA magnesium
RT transporters.";
RL J. Bacteriol. 180:2788-2791(1998).
RN [3]
RP FUNCTION, ACTIVITY REGULATION, INHIBITION BY CATION HEXAAMMINES, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10748031; DOI=10.1074/jbc.m001507200;
RA Kucharski L.M., Lubbe W.J., Maguire M.E.;
RT "Cation hexaammines are selective and potent inhibitors of the CorA
RT magnesium transport system.";
RL J. Biol. Chem. 275:16767-16773(2000).
RN [4]
RP SUBUNIT.
RX PubMed=15231793; DOI=10.1128/jb.186.14.4605-4612.2004;
RA Warren M.A., Kucharski L.M., Veenstra A., Shi L., Grulich P.F.,
RA Maguire M.E.;
RT "The CorA Mg2+ transporter is a homotetramer.";
RL J. Bacteriol. 186:4605-4612(2004).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-317 IN COMPLEX WITH MAGNESIUM
RP IONS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, MOTIF, AND DOMAIN.
RX PubMed=23091000; DOI=10.1073/pnas.1210076109;
RA Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J.,
RA Cornvik T., Phua T., Eshaghi S.;
RT "Structural insights into the mechanisms of Mg2+ uptake, transport, and
RT gating by CorA.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY (21.60 ANGSTROMS), SUBCELLULAR LOCATION,
RP SUBUNIT, AND DOMAIN.
RX PubMed=26051127; DOI=10.1016/j.bbamem.2015.06.002;
RA Cleverley R.M., Kean J., Shintre C.A., Baldock C., Derrick J.P., Ford R.C.,
RA Prince S.M.;
RT "The Cryo-EM structure of the CorA channel from Methanocaldococcus
RT jannaschii in low magnesium conditions.";
RL Biochim. Biophys. Acta 1848:2206-2215(2015).
CC -!- FUNCTION: Mediates influx of magnesium ions (PubMed:9573171,
CC PubMed:10748031). Alternates between open and closed states. Activated
CC by low cytoplasmic Mg(2+) levels. Inactive when cytoplasmic Mg(2+)
CC levels are high. Can also mediate Co(2+) uptake (By similarity).
CC {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:10748031,
CC ECO:0000269|PubMed:9573171}.
CC -!- ACTIVITY REGULATION: Inhibited by cation hexaammines.
CC {ECO:0000269|PubMed:10748031}.
CC -!- SUBUNIT: Homopentamer (PubMed:23091000, PubMed:26051127). In the
CC absence of Mg(2+), interactions between subunits are weakened, and
CC dimers, trimers and tetramers can be observed in vitro (By similarity).
CC Was initially proposed to be a homotetramer, based on the cross-linking
CC studies (PubMed:15231793). This is in contradiction with current 3D-
CC structures that clearly show it is a homopentamer (PubMed:23091000,
CC PubMed:26051127). {ECO:0000250|UniProtKB:Q9WZ31,
CC ECO:0000269|PubMed:15231793, ECO:0000269|PubMed:23091000,
CC ECO:0000269|PubMed:26051127}.
CC -!- INTERACTION:
CC Q58439; Q58439: corA; NbExp=2; IntAct=EBI-16019330, EBI-16019330;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10748031,
CC ECO:0000305|PubMed:26051127, ECO:0000305|PubMed:9573171}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:23091000,
CC ECO:0000269|PubMed:26051127}.
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 (PubMed:23091000). Low cytoplasmic Mg(2+) concentrations trigger both a
CC conformation change within each subunit and a loosening of the
CC interactions between subunits. This results in an open ion conduction
CC pathway. In addition, this results in a less symmetrical shape of the
CC whole complex (PubMed:26051127). {ECO:0000269|PubMed:23091000,
CC ECO:0000269|PubMed:26051127, ECO:0000305}.
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; L77117; AAB99037.1; -; Genomic_DNA.
DR PIR; H64428; H64428.
DR RefSeq; WP_010870546.1; NC_000909.1.
DR PDB; 4CY4; EM; 21.60 A; A/B/C/D/E=1-317.
DR PDB; 4EGW; X-ray; 2.50 A; A/B=1-258.
DR PDB; 4EV6; X-ray; 3.20 A; A/B/C/D/E=1-317.
DR PDBsum; 4CY4; -.
DR PDBsum; 4EGW; -.
DR PDBsum; 4EV6; -.
DR AlphaFoldDB; Q58439; -.
DR SMR; Q58439; -.
DR DIP; DIP-60086N; -.
DR STRING; 243232.MJ_1033; -.
DR TCDB; 1.A.35.3.1; the cora metal ion transporter (mit) family.
DR EnsemblBacteria; AAB99037; AAB99037; MJ_1033.
DR GeneID; 1451930; -.
DR KEGG; mja:MJ_1033; -.
DR eggNOG; arCOG02265; Archaea.
DR HOGENOM; CLU_007127_0_0_2; -.
DR InParanoid; Q58439; -.
DR OMA; GILHTDH; -.
DR OrthoDB; 43588at2157; -.
DR PhylomeDB; Q58439; -.
DR BRENDA; 7.2.2.14; 3260.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0050897; F:cobalt ion binding; IBA:GO_Central.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Ion transport; Magnesium; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..317
FT /note="Cobalt/magnesium transport protein CorA"
FT /id="PRO_0000201534"
FT TOPO_DOM 1..258
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:23091000"
FT TOPO_DOM 280..290
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:23091000"
FT TOPO_DOM 312..317
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT MOTIF 278..280
FT /note="Probable selectivity filter"
FT /evidence="ECO:0000305|PubMed:23091000"
FT SITE 254
FT /note="Essential for ion permeation"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT SITE 260
FT /note="Important for closing the ion permeation pathway in
FT the closed state"
FT /evidence="ECO:0000269|PubMed:23091000"
FT SITE 261
FT /note="Threonine that confers selectivity for Co(2+)
FT transport"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT STRAND 6..11
FT /evidence="ECO:0007829|PDB:4EGW"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 25..27
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 29..35
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 52..58
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 66..68
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 71..82
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 88..97
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:4EGW"
FT STRAND 125..127
FT /evidence="ECO:0007829|PDB:4EGW"
FT TURN 129..133
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 134..164
FT /evidence="ECO:0007829|PDB:4EGW"
FT TURN 165..167
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 171..203
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 211..248
FT /evidence="ECO:0007829|PDB:4EGW"
FT HELIX 269..276
FT /evidence="ECO:0007829|PDB:4EV6"
FT HELIX 292..312
FT /evidence="ECO:0007829|PDB:4EV6"
FT TURN 313..315
FT /evidence="ECO:0007829|PDB:4EV6"
SQ SEQUENCE 317 AA; 37142 MW; 552A0B3738131E0D CRC64;
MITVIAIAKD GSIVEPKLDE ISFEDYRLIW IDCYDPKDEE LYKLSKKIGI SVSDLQIGLD
EQEIPRVEED EDFYLIIYKA PLFEEDITTT SLGIYIKNNL LLTIHSDKIK AIGRLHKLIS
TKKPRIVFER GIGFLLYHIL NEITRSYSRI LMNLEDELEE LEDKLLAGYD REVMEKILGL
RKTLVYFHKS LIANRDVLVL LKRKYLPITT KEDRENFEDL YYDTLQLIDM SATYREVLTS
MMDITLSLEN IKMNQIMKIL TMVTTIFAVP MWITGIYGMN FSYLPLANNP QGFWLVMALM
VVIIMIFVYI FRRSGWI
