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Database: UniProt
Entry: J3Z504_9ENTR
LinkDB: J3Z504_9ENTR
Original site: J3Z504_9ENTR 
ID   J3Z504_9ENTR            Unreviewed;       316 AA.
AC   J3Z504;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=Magnesium transport protein CorA {ECO:0000256|ARBA:ARBA00019439, ECO:0000256|RuleBase:RU362010};
GN   Name=corA {ECO:0000256|RuleBase:RU362010};
GN   ORFNames=A35E_00033 {ECO:0000313|EMBL:AFP85359.1};
OS   secondary endosymbiont of Heteropsylla cubana.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; aphid secondary symbionts.
OX   NCBI_TaxID=134287 {ECO:0000313|EMBL:AFP85359.1, ECO:0000313|Proteomes:UP000003937};
RN   [1] {ECO:0000313|EMBL:AFP85359.1, ECO:0000313|Proteomes:UP000003937}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hcub_S {ECO:0000313|EMBL:AFP85359.1};
RX   PubMed=22821013; DOI=10.1093/molbev/mss180;
RA   Sloan D.B., Moran N.A.;
RT   "Genome reduction and co-evolution between the primary and secondary
RT   bacterial symbionts of psyllids.";
RL   Mol. Biol. Evol. 29:3781-3792(2012).
CC   -!- FUNCTION: Mediates influx of magnesium ions.
CC       {ECO:0000256|RuleBase:RU362010}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Mg(2+)(in) = Mg(2+)(out); Xref=Rhea:RHEA:29827,
CC         ChEBI:CHEBI:18420; Evidence={ECO:0000256|ARBA:ARBA00034269};
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362010}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141,
CC       ECO:0000256|RuleBase:RU362010}.
CC   -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC       family. {ECO:0000256|ARBA:ARBA00009765, ECO:0000256|RuleBase:RU362010}.
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DR   EMBL; CP003547; AFP85359.1; -; Genomic_DNA.
DR   RefSeq; WP_014888656.1; NC_018420.1.
DR   AlphaFoldDB; J3Z504; -.
DR   KEGG; sehc:A35E_00033; -.
DR   PATRIC; fig|134287.3.peg.34; -.
DR   HOGENOM; CLU_007127_5_0_6; -.
DR   OrthoDB; 9803416at2; -.
DR   Proteomes; UP000003937; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   CDD; cd12835; EcCorA-like_1; 1.
DR   Gene3D; 1.20.58.340; Magnesium transport protein CorA, transmembrane region; 1.
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   NCBIfam; TIGR00383; corA; 1.
DR   PANTHER; PTHR47685; MAGNESIUM TRANSPORT PROTEIN CORA; 1.
DR   PANTHER; PTHR47685:SF1; MAGNESIUM TRANSPORT PROTEIN CORA; 1.
DR   Pfam; PF01544; CorA; 1.
DR   SUPFAM; SSF143865; CorA soluble domain-like; 1.
DR   SUPFAM; SSF144083; Magnesium transport protein CorA, transmembrane region; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|RuleBase:RU362010};
KW   Ion transport {ECO:0000256|RuleBase:RU362010};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU362010};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362010};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003937};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362010};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362010}; Transport {ECO:0000256|RuleBase:RU362010}.
FT   TRANSMEM        255..278
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362010"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362010"
SQ   SEQUENCE   316 AA;  36458 MW;  1DFAEB7A77954F78 CRC64;
     MLNAFQLENH RLSRLDSDNS GSLSKAVWID LIEPGDHERK RVEKELGQSL ATRLELEDIE
     ASARFFENDD GLHIHSFFFY ADAEDHAGNA TVAFTIRDGR LYTLRERELP AFRLYRMRTR
     NQVLIDGNAY ELLLNLFETK IEQLADEIEN IYSDLEAVSL VIMDGHLGDE YDNAISTLAE
     LEDVAWKVRL CLMDTQRALN FLVRKTRLPG NQLEQAREVI RDIESLLPHN ESLFQKVNFL
     MQAAMGFINI EQNRIIKIFS VVSVVFLPPT LVASSYGMNF NFMPELRWSF GYPAAIILMI
     IAGLAPYLYF KQKKWL
//
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