FIEF_SHIFL
ID FIEF_SHIFL Reviewed; 300 AA.
AC Q83PD6; Q7UB82;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN OrderedLocusNames=SF3993, S3754;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN45427.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP18773.1; -; Genomic_DNA.
DR RefSeq; NP_709720.2; NC_004337.2.
DR RefSeq; WP_001076748.1; NZ_WPGW01000012.1.
DR AlphaFoldDB; Q83PD6; -.
DR SMR; Q83PD6; -.
DR STRING; 198214.SF3993; -.
DR EnsemblBacteria; AAN45427; AAN45427; SF3993.
DR EnsemblBacteria; AAP18773; AAP18773; S3754.
DR GeneID; 1025401; -.
DR GeneID; 58388831; -.
DR KEGG; sfl:SF3993; -.
DR KEGG; sfx:S3754; -.
DR PATRIC; fig|198214.7.peg.4705; -.
DR HOGENOM; CLU_013430_3_0_6; -.
DR OMA; IEMHLIV; -.
DR OrthoDB; 381612at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport; Zinc; Zinc transport.
FT CHAIN 1..300
FT /note="Cation-efflux pump FieF"
FT /id="PRO_0000206132"
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 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; 32913 MW; 6AF46DF777B1DC2E CRC64;
MNQSYGRLVS RAAIAATAMA SLLLLIKIFA WWYTGSVSIL AALVDSLVDI GASLTNLLVV
RYSLQPADDN HSFGHGKAES LAALAQSMFI SGSALFLFLT GIQHLVSPTP MTDPGVGVIV
TIVALICTII LVSFQRWVVR RTQSQAVRAD MLHYQSDVMM NGAILLALGL SWYGWHRADA
LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDEERQEIID IVTSWPGVSG AHDLRTRQSG
PTRFIQIHLE MEDSLPLVQA HMVADQVEQA ILRRFPGSDV IIHQDPCSVV PREGKRSMLS
