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CORA_HELHP
ID   CORA_HELHP              Reviewed;         322 AA.
AC   Q7VFJ7;
DT   30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Magnesium transport protein CorA;
GN   Name=corA; OrderedLocusNames=HH_1679;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
CC   -!- FUNCTION: Mediates influx of magnesium ions. Can also mediate cobalt
CC       and manganese uptake (By similarity). 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:P0ABI4, 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). {ECO:0000250|UniProtKB:Q9WZ31}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000250|UniProtKB:P0ABI4}; Multi-pass membrane protein
CC       {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; AE017125; AAP78276.1; -; Genomic_DNA.
DR   RefSeq; WP_011116518.1; NC_004917.1.
DR   AlphaFoldDB; Q7VFJ7; -.
DR   SMR; Q7VFJ7; -.
DR   STRING; 235279.HH_1679; -.
DR   EnsemblBacteria; AAP78276; AAP78276; HH_1679.
DR   KEGG; hhe:HH_1679; -.
DR   eggNOG; COG0598; Bacteria.
DR   HOGENOM; CLU_007127_5_0_7; -.
DR   OMA; RQNDDMR; -.
DR   OrthoDB; 822653at2; -.
DR   Proteomes; UP000002495; 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; IEA:InterPro.
DR   GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro.
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   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Magnesium; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..322
FT                   /note="Magnesium transport protein CorA"
FT                   /id="PRO_0000239096"
FT   TRANSMEM        264..284
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   MOTIF           283..285
FT                   /note="Probable selectivity filter"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
FT   SITE            259
FT                   /note="Essential for ion permeation"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WZ31"
SQ   SEQUENCE   322 AA;  37570 MW;  8595A8112FD98324 CRC64;
     MINIFIRRGG LIVRESLYSS DEQIKVFHEE DKILWIDLFR PSSDEVNYIS QTYHLEVPTK
     EEREEIEQSA RYWEDSGSIT INTYFLVRSL ESELHNETIT FLLRKNILFT IRYSEFRVFD
     EIQQIVLATP KVFEDGFDLI GKIFEIRVEK DADLLESAAK NTRALRKRVF NSQVINYDEM
     LEELSSLQEL NMSVRDSLFD KRRAITAVLK SDKADADVKK NITIVLKDLN SLVEFTAVNM
     HALDNIQTIL TNQINIEQNK TIKLFTVVTV AMMPPTLIGT IYGMNFDNMP ELHWDFSYPV
     ALVIMILSTI FPIIYFKKKG WI
 
 
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