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FIEF_YERPN
ID   FIEF_YERPN              Reviewed;         300 AA.
AC   Q1CD32; D1Q2D1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=Cation-efflux pump FieF {ECO:0000255|HAMAP-Rule:MF_01425};
GN   Name=fieF {ECO:0000255|HAMAP-Rule:MF_01425}; OrderedLocusNames=YPN_3771;
GN   ORFNames=YP516_4291;
OS   Yersinia pestis bv. Antiqua (strain Nepal516).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=377628;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RX   PubMed=16740952; DOI=10.1128/jb.00124-06;
RA   Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M.,
RA   Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516:
RT   evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nepal516;
RA   Plunkett G. III, Anderson B.D., Baumler D.J., Burland V., Cabot E.L.,
RA   Glasner J.D., Mau B., Neeno-Eckwall E., Perna N.T., Munk A.C., Tapia R.,
RA   Green L.D., Rogers Y.C., Detter J.C., Bruce D.C., Brettin T.S.;
RT   "Yersinia pestis Nepal516A whole genome shotgun sequencing project.";
RL   Submitted (APR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP000305; ABG20098.1; -; Genomic_DNA.
DR   EMBL; ACNQ01000019; EEO74684.1; -; Genomic_DNA.
DR   RefSeq; WP_002208967.1; NZ_ACNQ01000019.1.
DR   AlphaFoldDB; Q1CD32; -.
DR   SMR; Q1CD32; -.
DR   EnsemblBacteria; ABG20098; ABG20098; YPN_3771.
DR   GeneID; 66843532; -.
DR   KEGG; ypn:YPN_3771; -.
DR   HOGENOM; CLU_013430_3_0_6; -.
DR   OMA; IEMHLIV; -.
DR   Proteomes; UP000008936; 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_1000024333"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01425"
FT   TRANSMEM        40..60
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        155..175
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;  33396 MW;  4BD1F850941978B9 CRC64;
     MDPQYARWVK AAALSATALA SILLIIKIFA WWHTGSVSLL AALVDSLVDL AASLTNLFVV
     RYSLQPADEE HTFGHGKAES LAALAQSMFI SGSALFLFLT GFRHLASPEP LQDPSIGIGV
     TLVALFSTLI LVTFQRWVVR KTHSQAIRAD MLHYQSDVLM NGAILIALAL SWYGFRRADA
     LFALGIGVYI LYSALRMGYE AVQSLLDRAL PDDERQQIID IVTSWPGVIG AHDLRTRRSG
     QTRFIQLHLE MEDMMPLMEA HVLAEQVEHA LLYRFPGADV LIHQDPCSVV PKERHAHWEL
 
 
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