ID A0A1D8Y6Q2_9GAMM Unreviewed; 269 AA.
AC A0A1D8Y6Q2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN ORFNames=BIZ42_03000 {ECO:0000313|EMBL:AOX61253.1};
OS Stenotrophomonas sp. LM091.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas.
OX NCBI_TaxID=1904944 {ECO:0000313|EMBL:AOX61253.1, ECO:0000313|Proteomes:UP000177427};
RN [1] {ECO:0000313|EMBL:AOX61253.1, ECO:0000313|Proteomes:UP000177427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM091 {ECO:0000313|EMBL:AOX61253.1,
RC ECO:0000313|Proteomes:UP000177427};
RA Lefeuvre P.;
RT "Complete genome sequence of a copper-resistant commensal bacteria:
RT Stenotrophomonas sp. strain LM091.";
RL Submitted (SEP-2016) 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}.
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DR EMBL; CP017483; AOX61253.1; -; Genomic_DNA.
DR RefSeq; WP_070425510.1; NZ_CP017483.1.
DR AlphaFoldDB; A0A1D8Y6Q2; -.
DR STRING; 1904944.BIZ42_03000; -.
DR KEGG; slm:BIZ42_03000; -.
DR OrthoDB; 9787346at2; -.
DR Proteomes; UP000177427; 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 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 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 78..99
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 120..137
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 157..178
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 185..207
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 219..237
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 249..267
FT /note="Helical"
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 139
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 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 164
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 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 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 197
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 269 AA; 28499 MW; 3FBDD39B73080079 CRC64;
MPDISTENVW IALAVTLAAG LATALGSLMV LFSRRPNPRL LAFGLAFAGG AMVFVSLTEI
LNKAIDSFTQ AYDARLGFAY GTAAFLVGVL LIVVIDHLIP NPHESLDKQD PLFRDNNKAY
IKRVGLLTAV AITAHNFPEG LATFFATLES PSVGMPLAFA IAIHNIPEGI AIAVPVYFAT
QNKFYAFGAS LLSGLAEPIG AAIGYVALSG VLNHATFGWV FGIISGVMVF LALDELLPAA
KRYAKGHETV YGLVAGMGSL AISLVLFKW
//
