ID A0A0S8JNB7_9BACE Unreviewed; 272 AA.
AC A0A0S8JNB7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN ORFNames=AMS26_20555 {ECO:0000313|EMBL:KPL11174.1};
OS Bacteroides sp. SM23_62.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=1703352 {ECO:0000313|EMBL:KPL11174.1, ECO:0000313|Proteomes:UP000050819};
RN [1] {ECO:0000313|EMBL:KPL11174.1, ECO:0000313|Proteomes:UP000050819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_62 {ECO:0000313|EMBL:KPL11174.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPL11174.1}.
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DR EMBL; LJUP01000271; KPL11174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8JNB7; -.
DR PATRIC; fig|1703352.3.peg.2157; -.
DR Proteomes; UP000050819; 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..32
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 39..56
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 76..98
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 124..141
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 161..183
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 190..214
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 220..241
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 253..271
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT BINDING 140
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 143
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 143
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 168
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 169
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 172
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 172
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 201
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 272 AA; 29100 MW; 89C65F49CC9EFFCF CRC64;
MYTMEGSVLF AFGLTLFAGL STGIGSAMAF FTKSTNTRFL STALGFSAGV MIYVSFTEIL
GKSIQLLRES YGMTAGSWYA VLSFFGGILV IAIIDSMVPT FENPHEIRRV EDIRLHGQKN
QKSSLLRMGL FMAMAIAMHN VPEGLATFAA GMADPTIAIP IAVAIAIHNI PEGIAVSVPV
YYATGKKRKA FFLSFASGLA EPIGGILGWL FLSAVFNESI IGVLFGGVAG IMVFISVDEL
LPTAREYGHH HHAIYGLVAG MAIMAVSLLL FI
//
