FIEF_SALTI
ID FIEF_SALTI Reviewed; 298 AA.
AC Q8Z2W4; Q7C688;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN OrderedLocusNames=STY3810, t3558;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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, ECO:0000305}.
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DR EMBL; AL513382; CAD09563.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO71063.1; -; Genomic_DNA.
DR RefSeq; NP_457990.1; NC_003198.1.
DR RefSeq; WP_001077323.1; NZ_WSUR01000010.1.
DR AlphaFoldDB; Q8Z2W4; -.
DR SMR; Q8Z2W4; -.
DR STRING; 220341.16504677; -.
DR EnsemblBacteria; AAO71063; AAO71063; t3558.
DR KEGG; stt:t3558; -.
DR KEGG; sty:STY3810; -.
DR PATRIC; fig|220341.7.peg.3889; -.
DR eggNOG; COG0053; Bacteria.
DR HOGENOM; CLU_013430_3_0_6; -.
DR OMA; IEMHLIV; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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..298
FT /note="Cation-efflux pump FieF"
FT /id="PRO_0000206130"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT TRANSMEM 112..132
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT TRANSMEM 176..196
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 151
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
SQ SEQUENCE 298 AA; 32742 MW; FAA9B3DE2A610840 CRC64;
MNQTYGRLVS RAAIAATAMA SALLLIKIFA WWYTGSVSIL AALVDSLVDI AASLTNLLVV
RYSLQPADDE HTFGHGKAES LAALAQSMFI SGSALFLTSI QNLIKPTPMN DPGVGIGVTV
IALICTIILV TFQRWVVRKT QSQAVRADML HYQSDVMMNG AILIALGLSW YGWHRADALF
ALGIGIYILY SALRMGYEAV QSLLDRALPD AERQEIIDIV TSWPGVSGAH DLRTRQSGPT
RFIQIHLEME DNLPLVQAHF VADQVEQAIL RRFPGSDVII HQDPCSVVPR EGRKFELV
