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FIEF_SALEP
ID   FIEF_SALEP              Reviewed;         300 AA.
AC   B5QWZ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN   Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425}; OrderedLocusNames=SEN3851;
OS   Salmonella enteritidis PT4 (strain P125109).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=550537;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P125109;
RX   PubMed=18583645; DOI=10.1101/gr.077404.108;
RA   Thomson N.R., Clayton D.J., Windhorst D., Vernikos G., Davidson S.,
RA   Churcher C., Quail M.A., Stevens M., Jones M.A., Watson M., Barron A.,
RA   Layton A., Pickard D., Kingsley R.A., Bignell A., Clark L., Harris B.,
RA   Ormond D., Abdellah Z., Brooks K., Cherevach I., Chillingworth T.,
RA   Woodward J., Norberczak H., Lord A., Arrowsmith C., Jagels K., Moule S.,
RA   Mungall K., Saunders M., Whitehead S., Chabalgoity J.A., Maskell D.,
RA   Humphreys T., Roberts M., Barrow P.A., Dougan G., Parkhill J.;
RT   "Comparative genome analysis of Salmonella enteritidis PT4 and Salmonella
RT   gallinarum 287/91 provides insights into evolutionary and host adaptation
RT   pathways.";
RL   Genome Res. 18:1624-1637(2008).
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; AM933172; CAR35424.1; -; Genomic_DNA.
DR   RefSeq; WP_001077320.1; NC_011294.1.
DR   AlphaFoldDB; B5QWZ4; -.
DR   SMR; B5QWZ4; -.
DR   KEGG; set:SEN3851; -.
DR   HOGENOM; CLU_013430_3_0_6; -.
DR   OMA; IEMHLIV; -.
DR   Proteomes; UP000000613; 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: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_1000145701"
FT   TRANSMEM        24..44
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        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        178..198
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;  32974 MW;  32A5AE73F921786F CRC64;
     MNQTYGRLVS RAAIAATAMA SALLLIKIFA WWYTGSVSIL AALVDSLVDI AASLTNLLVV
     RYSLQPADDE HTFGHGKAES LAALAQSMFI SGSALFLFLT SIQNLIKPTP MNDPGVGIGV
     TVIALICTII LVTFQRWVVR KTQSQAVRAD MLHYQSDVMM NGAILIALGL SWYGWHRADA
     LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDAERQEIID IVTSWPGVSG AHDLRTRQSG
     PTRFIQIHLE MEDNLPLVQA HFVADQVEQA ILQRFPGSDV IIHQDPCSVV PREGRKFELV
 
 
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