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Database: UniProt
Entry: A0A0K8R0C0_9BACT
LinkDB: A0A0K8R0C0_9BACT
Original site: A0A0K8R0C0_9BACT 
ID   A0A0K8R0C0_9BACT        Unreviewed;       275 AA.
AC   A0A0K8R0C0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN   Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN   ORFNames=BA6E_124201 {ECO:0000313|EMBL:GAP70386.1};
OS   Bacteroidales bacterium 6E.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1688776 {ECO:0000313|EMBL:GAP70386.1, ECO:0000313|Proteomes:UP000251980};
RN   [1] {ECO:0000313|Proteomes:UP000251980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=6E {ECO:0000313|Proteomes:UP000251980};
RA   Tourlousse D.M., Honda T., Matsuura N., Ohashi A., Tonouchi A.,
RA   Sekiguchi Y.;
RT   "Draft Genome Sequence of Bacteroidales Strain 6E, Isolated from a Rice
RT   Paddy Field in Japan.";
RL   Genome Announc. 3:e01167-e01115(2015).
CC   -!- FUNCTION: Mediates zinc uptake. May also transport other divalent
CC       cations. {ECO:0000256|HAMAP-Rule:MF_00548}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Zn(2+)(in) = Zn(2+)(out); Xref=Rhea:RHEA:29351,
CC         ChEBI:CHEBI:29105; Evidence={ECO:0000256|HAMAP-Rule:MF_00548};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00548};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00548}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. ZupT
CC       subfamily. {ECO:0000256|ARBA:ARBA00009703, ECO:0000256|HAMAP-
CC       Rule:MF_00548}.
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DR   EMBL; DF970689; GAP70386.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K8R0C0; -.
DR   STRING; 1688776.GCA_001270045_02847; -.
DR   Proteomes; UP000251980; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005385; F:zinc ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00548; ZupT; 1.
DR   InterPro; IPR003689; ZIP.
DR   InterPro; IPR023498; Zn_transptr_ZupT.
DR   PANTHER; PTHR11040:SF205; ZINC-REGULATED TRANSPORTER 3; 1.
DR   PANTHER; PTHR11040; ZINC/IRON TRANSPORTER; 1.
DR   Pfam; PF02535; Zip; 2.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00548};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065, ECO:0000256|HAMAP-
KW   Rule:MF_00548}; Iron {ECO:0000256|ARBA:ARBA00023004};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00548};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000251980};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00548};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00548};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00548};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00548};
KW   Zinc transport {ECO:0000256|ARBA:ARBA00022906, ECO:0000256|HAMAP-
KW   Rule:MF_00548}.
FT   TRANSMEM        6..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        38..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        76..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        160..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        189..211
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        223..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   TRANSMEM        255..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         139
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /note="M2 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         142
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /note="M1 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         142
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /note="M2 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         167
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /note="M1 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         168
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /note="M2 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         171
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /note="M1 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         171
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /note="M2 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT   BINDING         200
FT                   /ligand="Fe(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29033"
FT                   /note="M2 metal binding site"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
SQ   SEQUENCE   275 AA;  29628 MW;  8F41095153EF1E59 CRC64;
     MMEEGNFLLA FLLTLFAGLS TGIGSTIAFL AKRTNTKLLS FALGFSAGVM IYISFVEIFP
     DARSTFIEKF GEFNGTLYTL TSFFGGMLLI AMIDKFIPSA ENPHEMRSVE SMDNEKKALN
     FRKLYRLGIM TSLAVGIHNF PEGIATFMSV MKDPGLGVAI AIAIAIHNIP EGIAVSVPVY
     YATGDRKKAF MLSFLSGLSE PIGALIAYLL LIPLLDSGSF DVVFGAVMAG IAGIMVFISL
     DELLPSAEEY GEHHIAIYGL TGGMGVMALS LLFLI
//
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