ID A0A124FXJ9_9BACT Unreviewed; 264 AA.
AC A0A124FXJ9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 23.
DE RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN ORFNames=XD94_1794 {ECO:0000313|EMBL:KUK78235.1};
OS Mesotoga prima.
OC Bacteria; Thermotogota; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX NCBI_TaxID=1184387 {ECO:0000313|EMBL:KUK78235.1, ECO:0000313|Proteomes:UP000054092};
RN [1] {ECO:0000313|Proteomes:UP000054092}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26787827; DOI=10.1128/mbio.01669-15;
RA Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA Andersen G.L., Banfield J.F.;
RT "Genome-Resolved Metagenomic Analysis Reveals Roles for Candidate Phyla and
RT Other Microbial Community Members in Biogeochemical Transformations in Oil
RT Reservoirs.";
RL MBio 7:e01669-15(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUK78235.1}.
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DR EMBL; LGGP01000398; KUK78235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A124FXJ9; -.
DR PATRIC; fig|1184387.3.peg.238; -.
DR Proteomes; UP000054092; 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; 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 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..30
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 37..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 79..96
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 117..134
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 212..233
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT BINDING 133
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 136
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 136
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 161
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 162
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 165
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 165
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 194
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 264 AA; 27983 MW; 98D75E8909B6B116 CRC64;
MQLDNFWPAF FLTVFAGLST GIGSILAIFA KKTNTKFLSV SLGFSAGIMI YVSFVEIFVK
SGESLQKSVG SGISDWINVI AFFGGIGIIA LIDFLVPSAE NPHEMRDVDE MQAKSKTLLR
MGLFTAFAIA VHNFPEGLAT FLAAMKDPSL GVPIAVAIAI HNVPEGIAVA VPIYHATGSR
KKAFMYSFLS GLAEPAGALI GFALINILFT DIAFGIVFAG VAGIMVYISL DELLPSAEKY
GEHHLSISGL IAGMGLMAVS LLIL
//
