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FIEF_ESCF3
ID   FIEF_ESCF3              Reviewed;         300 AA.
AC   B7LVD0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN   Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425}; OrderedLocusNames=EFER_3858;
OS   Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CCUG 18766 / IAM
OS   14443 / JCM 21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585054;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35469 / DSM 13698 / BCRC 15582 / CCUG 18766 / IAM 14443 / JCM
RC   21226 / LMG 7866 / NBRC 102419 / NCTC 12128 / CDC 0568-73;
RX   PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA   Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA   Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA   Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA   Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA   Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA   Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA   Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT   "Organised genome dynamics in the Escherichia coli species results in
RT   highly diverse adaptive paths.";
RL   PLoS Genet. 5:E1000344-E1000344(2009).
CC   -!- FUNCTION: Divalent metal cation transporter which exports Zn(2+),
CC       Cd(2+) and possibly Fe(2+). May be involved in zinc and iron
CC       detoxification by efflux. {ECO:0000255|HAMAP-Rule:MF_01425}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out);
CC         Xref=Rhea:RHEA:28839, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01425};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Cd(2+)(in) + H(+)(out) = Cd(2+)(out) + H(+)(in);
CC         Xref=Rhea:RHEA:28739, ChEBI:CHEBI:15378, ChEBI:CHEBI:48775;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01425};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Fe(2+)(in) + H(+)(out) = Fe(2+)(out) + H(+)(in);
CC         Xref=Rhea:RHEA:29439, ChEBI:CHEBI:15378, ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01425};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01425}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01425}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01425}.
CC   -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF)
CC       transporter (TC 2.A.4) family. FieF subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01425}.
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DR   EMBL; CU928158; CAQ91293.1; -; Genomic_DNA.
DR   RefSeq; WP_001076736.1; NC_011740.1.
DR   AlphaFoldDB; B7LVD0; -.
DR   SMR; B7LVD0; -.
DR   EnsemblBacteria; CAQ91293; CAQ91293; EFER_3858.
DR   GeneID; 60902734; -.
DR   KEGG; efe:EFER_3858; -.
DR   HOGENOM; CLU_013430_3_0_6; -.
DR   OMA; IEMHLIV; -.
DR   OrthoDB; 381612at2; -.
DR   BioCyc; EFER585054:EFER_RS19275-MON; -.
DR   Proteomes; UP000000745; 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:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW.
DR   GO; GO:0006826; P:iron ion transport; IEA:InterPro.
DR   GO; GO:0006829; P:zinc ion transport; IEA:InterPro.
DR   Gene3D; 1.20.1510.10; -; 1.
DR   Gene3D; 3.30.70.1350; -; 1.
DR   HAMAP; MF_01425; Cation_efflux_FieF; 1.
DR   InterPro; IPR002524; Cation_efflux.
DR   InterPro; IPR027470; Cation_efflux_CTD.
DR   InterPro; IPR036837; Cation_efflux_CTD_sf.
DR   InterPro; IPR023783; Cation_efflux_FieF.
DR   InterPro; IPR027469; Cation_efflux_TMD_sf.
DR   Pfam; PF01545; Cation_efflux; 1.
DR   Pfam; PF16916; ZT_dimer; 1.
DR   SUPFAM; SSF160240; SSF160240; 1.
DR   SUPFAM; SSF161111; SSF161111; 1.
DR   TIGRFAMs; TIGR01297; CDF; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Ion transport; Iron; Iron transport;
KW   Membrane; Metal-binding; Transmembrane; Transmembrane helix; Transport;
KW   Zinc; Zinc transport.
FT   CHAIN           1..300
FT                   /note="Cation-efflux pump FieF"
FT                   /id="PRO_1000145697"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        82..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        172..192
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   BINDING         45
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   BINDING         49
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   BINDING         153
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
SQ   SEQUENCE   300 AA;  32929 MW;  DD069C7669E95033 CRC64;
     MNQSYGRLVS RAAIAATAMA SLLLLIKIFA WWYTGSVSIL AALVDSLVDI GASLTNLLVV
     RYSLQPADDN HSFGHGKAES LAALAQSMFI SGSALFLFLT GIQHLISPTP MNDPGVGIIV
     TIVALVCTIL LVSFQRWVVR RTQSQAVRAD MLHYQSDVMM NGAILLALAL SWYGWHSADA
     LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDDERQEIID IVTSWPGVSG AHDLRTRQSG
     PTRFIQIHLE MEDSLPLVQA HMVADQVEQA ILRRFPGSDV IIHQDPCSVV PREGKRFELS
 
 
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