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FIEF_ECOLU
ID   FIEF_ECOLU              Reviewed;         300 AA.
AC   B7NFL2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN   Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425}; OrderedLocusNames=ECUMN_4443;
OS   Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585056;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMN026 / ExPEC;
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; CU928163; CAR15569.1; -; Genomic_DNA.
DR   RefSeq; WP_001076742.1; NC_011751.1.
DR   RefSeq; YP_002415058.1; NC_011751.1.
DR   AlphaFoldDB; B7NFL2; -.
DR   SMR; B7NFL2; -.
DR   STRING; 585056.ECUMN_4443; -.
DR   EnsemblBacteria; CAR15569; CAR15569; ECUMN_4443.
DR   GeneID; 66672177; -.
DR   KEGG; eum:ECUMN_4443; -.
DR   PATRIC; fig|585056.7.peg.4612; -.
DR   HOGENOM; CLU_013430_3_0_6; -.
DR   OMA; IEMHLIV; -.
DR   Proteomes; UP000007097; 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_1000145694"
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;  32927 MW;  A9ECC4D6ED9A750F CRC64;
     MNQSYGRLVS RAAIAATAMA SLLLLIKIFA WWYTGSVSIL AALVDSLVDI GASLTNLLVV
     RYSLQPADDN HSFGHGKAES LAALAQSMFI SGSALFLFLT GIQHLISPTP MTDPGVGVIV
     TIVALICTII LVSFQRWVVR RTQSQAVRAD MLHYQSDVMM NGAILLALGL SWYGWHRADA
     LFALGIGIYI LYSALRMGYE AVQSLLDRAL PDEERQEIID IVTSWPGVSG AHDLRTRQSG
     PTRFIQIHLE MEDSLPLVQA HMVADQVEQA ILRRFPGSDV IIHQDPCSVV PREGKRSMLS
 
 
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