CORA_BACSU
ID CORA_BACSU Reviewed; 317 AA.
AC P40948;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Magnesium transport protein CorA;
GN Name=corA; Synonyms=yqhC, yqxL; OrderedLocusNames=BSU24740;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / JH642;
RX PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA Kobayashi Y.;
RT "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT Bacillus subtilis genome containing the skin element and many sporulation
RT genes.";
RL Microbiology 142:3103-3111(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-317.
RX PubMed=2507524; DOI=10.1128/jb.171.10.5386-5404.1989;
RA Albano M., Breitling R., Dubnau D.A.;
RT "Nucleotide sequence and genetic organization of the Bacillus subtilis comG
RT operon.";
RL J. Bacteriol. 171:5386-5404(1989).
RN [4]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
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 INDUCTION.
RX PubMed=15856219; DOI=10.1007/s00253-005-1898-1;
RA Hyyrylaeinen H.-L., Sarvas M., Kontinen V.P.;
RT "Transcriptome analysis of the secretion stress response of Bacillus
RT subtilis.";
RL Appl. Microbiol. Biotechnol. 67:389-396(2005).
CC -!- FUNCTION: Mediates influx of magnesium ions. Alternates between open
CC and closed states. Activated by low cytoplasmic Mg(2+) levels. Inactive
CC when cytoplasmic Mg(2+) levels are high. May also mediate uptake of
CC Co(2+). {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). Homotetramer (PubMed:15231793).
CC {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000305|PubMed:15231793}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15231793};
CC Multi-pass membrane protein {ECO:0000305}.
CC -!- INDUCTION: By secretion stress. {ECO:0000269|PubMed:15856219}.
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 Low Mg(2+) concentrations trigger both a conformation change within
CC each subunit and a loosening of the interactions between subunits. This
CC results in an open ion conduction pathway. In addition, this results in
CC a less symmetrical shape of the whole complex.
CC {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; D84432; BAA12532.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14405.1; -; Genomic_DNA.
DR EMBL; M29691; AAA83366.1; -; Genomic_DNA.
DR PIR; F69968; F69968.
DR RefSeq; NP_390354.1; NC_000964.3.
DR RefSeq; WP_004399136.1; NZ_CP053102.1.
DR AlphaFoldDB; P40948; -.
DR SMR; P40948; -.
DR STRING; 224308.BSU24740; -.
DR TCDB; 1.A.35.1.3; the cora metal ion transporter (mit) family.
DR PaxDb; P40948; -.
DR PRIDE; P40948; -.
DR EnsemblBacteria; CAB14405; CAB14405; BSU_24740.
DR GeneID; 938517; -.
DR KEGG; bsu:BSU24740; -.
DR PATRIC; fig|224308.179.peg.2693; -.
DR eggNOG; COG0598; Bacteria.
DR InParanoid; P40948; -.
DR OMA; YHIRHEL; -.
DR PhylomeDB; P40948; -.
DR BioCyc; BSUB:BSU24740-MON; -.
DR Proteomes; UP000001570; 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: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; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR Pfam; PF01544; CorA; 1.
DR SUPFAM; SSF143865; SSF143865; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Ion transport; Magnesium; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..317
FT /note="Magnesium transport protein CorA"
FT /id="PRO_0000049850"
FT TRANSMEM 240..260
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MOTIF 259..261
FT /note="Probable selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT SITE 235
FT /note="Essential for ion permeation"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT SITE 241
FT /note="Important for closing the ion permeation pathway in
FT the closed state"
FT /evidence="ECO:0000250|UniProtKB:Q9WZ31"
SQ SEQUENCE 317 AA; 37708 MW; B92E39557AED0834 CRC64;
MKAHTGKDWF WYQMGPQERS KARDLIHFSH WPQCEKWFEN NHHVNFLRVD TTETENEAVF
GSIVYDQGLG EEKDHTVFHF YITRQYFFTI NFDFSILREI KGKEVVRQME RADNAIEGFL
ILLGELMNAY LIGVDEFEVK LRKLRWQIKD DNSKSILNRV HLLRHELMIW KNLILSAKKI
EMALKETFLP QNEGKKDYQR TQLKIDRGFT YISEFEGELN NLLHSEEVIT SHRGNEIVKA
LTIFTTLFTP ITALGALWGM NFSVMPELNW KYGYLFSLLL IVTSTVLIYL YLRKKGWTGD
MLQERKKKKK PRKRRTL
