FIEF_SALPA
ID FIEF_SALPA Reviewed; 300 AA.
AC Q5PIR7;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425}; OrderedLocusNames=SPA3904;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000026; AAV79670.1; -; Genomic_DNA.
DR RefSeq; WP_001077325.1; NC_006511.1.
DR AlphaFoldDB; Q5PIR7; -.
DR SMR; Q5PIR7; -.
DR EnsemblBacteria; AAV79670; AAV79670; SPA3904.
DR KEGG; spt:SPA3904; -.
DR HOGENOM; CLU_013430_3_0_6; -.
DR OMA; IEMHLIV; -.
DR Proteomes; UP000008185; 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_0000206129"
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; 32968 MW; 31254E7704D8786D CRC64;
MNQTYGRLVS RAAIAATAMA SALLLIKILA WWYTGSVSIL AALVDSLVDI AASLTNLLVV
RYSLQPADDE HTFGHGKAES LAALAQSMFI SGSALFLFLT SIQNLIKPTP MNDPGVGIGV
TVIALICTII LVTFQRWVVR KTQSQAVRAD MLHYQSDVMM NGAILIALGL SWYGWHRADA
LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDAERQEIID IVTSWPGVSG AHDLRTRQSG
PTRFIQIHLE MEDNLPLVQA HFVADQVEQA ILRRFPGSDV IIHQDPCSVV PREGRKFELV
