ID A0A094RJU4_9ACTN Unreviewed; 269 AA.
AC A0A094RJU4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 08-NOV-2023, entry version 31.
DE RecName: Full=Zinc transporter ZupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000256|HAMAP-Rule:MF_00548};
GN ORFNames=GM43_3195 {ECO:0000313|EMBL:KGA05028.1};
OS actinobacterium acMicro-4.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504317 {ECO:0000313|EMBL:KGA05028.1, ECO:0000313|Proteomes:UP000029304};
RN [1] {ECO:0000313|EMBL:KGA05028.1, ECO:0000313|Proteomes:UP000029304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) 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}.
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:KGA05028.1}.
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DR EMBL; JNSD01000012; KGA05028.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094RJU4; -.
DR STRING; 1504317.GM43_3195; -.
DR PATRIC; fig|1504317.4.peg.641; -.
DR Proteomes; UP000029304; 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 29..50
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 71..91
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 153..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 186..209
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 215..236
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00548"
FT TRANSMEM 248..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; 28054 MW; FBED2021EF160E4B CRC64;
MVFAGLVTLG AGLATAVGAA IGLFAHHTNR AFLALALGFS AGVMIYVSFI EIIPKATSYL
VADRGDAFGN TIMAGTFLAG LAVMALLYRF LPDLEHPQLD DRHEALSLDE DPSSYYANRP
LLKAGIGVAL AVTLHNFPEG MATFFLTLDD PQVGLSVALA IAIHNLPEGI AVAVPIYYAT
KSRAKAFAFG ALSGLAEPIG AFIGFAILQP FITDTVLGIV FAAVAGVMVY ISVDSLLPAA
RQYGRGQLAI YGLIAGMAVM AGSLVLFSL
//
