CORA_ECOLI
ID CORA_ECOLI Reviewed; 316 AA.
AC P0ABI4; P27841; Q2M8C1;
DT 25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; OrderedLocusNames=b3816, JW3789;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=8314774; DOI=10.1016/s0021-9258(19)85210-9;
RA Smith R.L., Banks J.L., Snavely M.D., Maguire M.E.;
RT "Sequence and topology of the CorA magnesium transport systems of
RT Salmonella typhimurium and Escherichia coli. Identification of a new class
RT of transport protein.";
RL J. Biol. Chem. 268:14071-14080(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Ohmori H.;
RT "Physical map of the corA region of the E.coli chromosome.";
RL Submitted (JAN-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=1379743; DOI=10.1126/science.1379743;
RA Daniels D.L., Plunkett G. III, Burland V.D., Blattner F.R.;
RT "Analysis of the Escherichia coli genome: DNA sequence of the region from
RT 84.5 to 86.5 minutes.";
RL Science 257:771-778(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8346018; DOI=10.1093/nar/21.15.3391;
RA Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome. III. DNA sequence of the region
RT from 87.2 to 89.2 minutes.";
RL Nucleic Acids Res. 21:3391-3398(1993).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=780341; DOI=10.1128/jb.126.3.1096-1103.1976;
RA Park M.H., Wong B.B., Lusk J.E.;
RT "Mutants in three genes affecting transport of magnesium in Escherichia
RT coli: genetics and physiology.";
RL J. Bacteriol. 126:1096-1103(1976).
RN [8]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Mediates influx of magnesium ions. Can also mediate cobalt
CC and manganese uptake (PubMed:780341). 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:Q9WZ31, ECO:0000269|PubMed:780341}.
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|PubMed:780341};
CC Multi-pass 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; L11042; AAB59046.1; -; Genomic_DNA.
DR EMBL; L02122; AAD15038.1; -; Genomic_DNA.
DR EMBL; M87049; AAA67612.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76819.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77485.1; -; Genomic_DNA.
DR PIR; A65186; B47157.
DR RefSeq; NP_418260.1; NC_000913.3.
DR RefSeq; WP_000947159.1; NZ_STEB01000021.1.
DR PDB; 5N77; X-ray; 2.80 A; A/B/C/D/E=1-257.
DR PDB; 5N78; X-ray; 2.85 A; A/B/C/D/E=1-257.
DR PDBsum; 5N77; -.
DR PDBsum; 5N78; -.
DR AlphaFoldDB; P0ABI4; -.
DR SMR; P0ABI4; -.
DR BioGRID; 4263113; 42.
DR IntAct; P0ABI4; 4.
DR STRING; 511145.b3816; -.
DR TCDB; 1.A.35.1.1; the cora metal ion transporter (mit) family.
DR jPOST; P0ABI4; -.
DR PaxDb; P0ABI4; -.
DR PRIDE; P0ABI4; -.
DR EnsemblBacteria; AAC76819; AAC76819; b3816.
DR EnsemblBacteria; BAE77485; BAE77485; BAE77485.
DR GeneID; 66672278; -.
DR GeneID; 948351; -.
DR KEGG; ecj:JW3789; -.
DR KEGG; eco:b3816; -.
DR PATRIC; fig|511145.12.peg.3932; -.
DR EchoBASE; EB1431; -.
DR eggNOG; COG0598; Bacteria.
DR HOGENOM; CLU_007127_5_0_6; -.
DR InParanoid; P0ABI4; -.
DR OMA; RQNDDMR; -.
DR PhylomeDB; P0ABI4; -.
DR BioCyc; EcoCyc:CORA-MON; -.
DR BioCyc; MetaCyc:CORA-MON; -.
DR PRO; PR:P0ABI4; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IDA:EcoCyc.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006824; P:cobalt ion transport; IDA:EcoCyc.
DR GO; GO:0015693; P:magnesium ion transport; IDA:EcoCyc.
DR GO; GO:0035444; P:nickel cation transmembrane transport; IDA:EcoCyc.
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 inner membrane; Cell membrane; Cobalt; Ion transport;
KW Magnesium; Manganese; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..316
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000201527"
FT TOPO_DOM 1..254
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 255..273
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 274..287
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 288..310
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 311..316
FT /note="Cytoplasmic"
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"
FT CONFLICT 49..50
FT /note="SL -> RP (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="G -> A (in Ref. 1; AAB59046)"
FT /evidence="ECO:0000305"
FT STRAND 2..10
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 12..15
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 27..33
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 65..68
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 71..81
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:5N77"
FT STRAND 100..107
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 110..119
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 129..164
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 169..205
FT /evidence="ECO:0007829|PDB:5N77"
FT HELIX 210..256
FT /evidence="ECO:0007829|PDB:5N77"
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
