CORC_SALTY
ID CORC_SALTY Reviewed; 292 AA.
AC P0A2L3; O87575; Q9R874;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Magnesium and cobalt efflux protein CorC;
GN Name=corC; OrderedLocusNames=STM0667;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RA Smith R.L., Ahuga D., Thacker L.K., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: sequence and
RT characterization of the corB, corC, and corD genes.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 20-292.
RC STRAIN=LEU485;
RA Gupta S.D., Rahman A., Wu H.C., Rick P.D.;
RT "Cloning and sequencing of apolipoprotein N-acyltransferase from Salmonella
RT typhimurium.";
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION.
RX PubMed=1779764; DOI=10.1111/j.1365-2958.1991.tb01984.x;
RA Gibson M.M., Bagga D.A., Miller C.G., Maguire M.E.;
RT "Magnesium transport in Salmonella typhimurium: the influence of new
RT mutations conferring Co2+ resistance on the CorA Mg2+ transport system.";
RL Mol. Microbiol. 5:2753-2762(1991).
CC -!- FUNCTION: Plays a role in the transport of magnesium and cobalt ions.
CC {ECO:0000250, ECO:0000269|PubMed:1779764}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. {ECO:0000305}.
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DR EMBL; AF085347; AAC36474.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL19618.1; -; Genomic_DNA.
DR EMBL; AF116773; AAD09823.1; -; Genomic_DNA.
DR RefSeq; NP_459659.1; NC_003197.2.
DR RefSeq; WP_001278615.1; NC_003197.2.
DR PDB; 3NQR; X-ray; 2.00 A; A/B/C/D=65-191.
DR PDBsum; 3NQR; -.
DR AlphaFoldDB; P0A2L3; -.
DR SMR; P0A2L3; -.
DR STRING; 99287.STM0667; -.
DR TCDB; 1.C.126.1.2; the hlyc haemolysin (hlyc) family.
DR PaxDb; P0A2L3; -.
DR DNASU; 1252187; -.
DR EnsemblBacteria; AAL19618; AAL19618; STM0667.
DR GeneID; 1252187; -.
DR KEGG; stm:STM0667; -.
DR PATRIC; fig|99287.12.peg.703; -.
DR HOGENOM; CLU_015237_3_0_6; -.
DR OMA; ERRHMAL; -.
DR PhylomeDB; P0A2L3; -.
DR BioCyc; SENT99287:STM0667-MON; -.
DR EvolutionaryTrace; P0A2L3; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR Pfam; PF00571; CBS; 2.
DR Pfam; PF03471; CorC_HlyC; 1.
DR SMART; SM00116; CBS; 2.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51371; CBS; 2.
PE 1: Evidence at protein level;
KW 3D-structure; CBS domain; Cobalt; Magnesium; Reference proteome; Repeat;
KW Transport.
FT CHAIN 1..292
FT /note="Magnesium and cobalt efflux protein CorC"
FT /id="PRO_0000088351"
FT DOMAIN 73..133
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 135..195
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT CONFLICT 122
FT /note="L -> F (in Ref. 1; AAC36474)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="E -> V (in Ref. 1; AAC36474)"
FT /evidence="ECO:0000305"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 76..78
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 88..98
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 119..126
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 135..138
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 144..146
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 151..160
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:3NQR"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:3NQR"
FT HELIX 181..187
FT /evidence="ECO:0007829|PDB:3NQR"
SQ SEQUENCE 292 AA; 33299 MW; 54831AFCFACD2FBE CRC64;
MSDDNSHSSD TVNSKKGFFS LLLSQLFHGE PKNRDELLAL IRDSGQNELI DEDTRDMLEG
VMDIADQRVR DIMIPRSQMI TLKRNQTLDE CLDVIIESAH SRFPVISEDK DHIEGILMAK
DLLPFMRSDA EAFSMDKVLR TAVVVPESKR VDRMLKEFRS QRYHMAIVID EFGGVSGLVT
IEDILELIVG EIEDEYDEED DIDFRQLSRH TWTIRALASI EDFNDAFGTH FSDEEVDTIG
GLVMQAFGHL PARGETIDID GYQFKVAMAD SRRIIQVHVR IPDDSPQPKL DE