ID L0K8R6_HALHC Unreviewed; 270 AA.
AC L0K8R6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN OrderedLocusNames=Halha_0777 {ECO:0000313|EMBL:AGB40749.1};
OS Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC Halobacteroides.
OX NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB40749.1, ECO:0000313|Proteomes:UP000010880};
RN [1] {ECO:0000313|Proteomes:UP000010880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC {ECO:0000313|Proteomes:UP000010880};
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "The complete genome of Halobacteroides halobius DSM 5150.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00548}.
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DR EMBL; CP003359; AGB40749.1; -; Genomic_DNA.
DR RefSeq; WP_015326474.1; NC_019978.1.
DR AlphaFoldDB; L0K8R6; -.
DR STRING; 748449.Halha_0777; -.
DR KEGG; hhl:Halha_0777; -.
DR PATRIC; fig|748449.3.peg.735; -.
DR eggNOG; COG0428; Bacteria.
DR HOGENOM; CLU_015114_1_3_9; -.
DR OrthoDB; 9787346at2; -.
DR Proteomes; UP000010880; Chromosome.
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; 1.
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:UP000010880};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 35..57
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 72..90
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 217..240
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 252..269
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 270 AA; 29264 MW; 0F0A6C4B6575755F CRC64;
MNNFSIAFLL TLFAGLATGI GSVLVLFIKD VKKSFLSISL GFSAGVMIYV SFIEIFFKAQ
ESLVSYLGVR NGKIVTVVSF FLGVLMIGLI DKLVPDIENP HHAHNQNGAN NLEQERGVDE
DAQLLRMGAF SALAIAIHNF PEGLATFASA LKDPSLGIPI AIAIAIHNIP EGISVSVPVY
YATKDKKKAF FYSFLSGLSE PIGAFIGYFL LRSFFNDLVF GILFGMVAGI MVFISIDELL
PTSRNYGQGH QEIYGFVAGM AVMAVSLLLF
//
