ID ZUPT_CAMJE Reviewed; 291 AA.
AC Q9PIN2; Q0PBP2;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE RecName: Full=Zinc transporter ZupT {ECO:0000255|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000255|HAMAP-Rule:MF_00548}; OrderedLocusNames=Cj0263;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
CC -!- FUNCTION: Mediates zinc uptake. May also transport other divalent
CC cations. {ECO:0000255|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:0000255|HAMAP-Rule:MF_00548};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_00548}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_00548, ECO:0000305}.
CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. ZupT
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00548, ECO:0000305}.
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DR EMBL; AL111168; CAL34417.1; -; Genomic_DNA.
DR PIR; F81444; F81444.
DR RefSeq; WP_002851840.1; NZ_SZUC01000004.1.
DR RefSeq; YP_002343705.1; NC_002163.1.
DR AlphaFoldDB; Q9PIN2; -.
DR SMR; Q9PIN2; -.
DR IntAct; Q9PIN2; 1.
DR STRING; 192222.Cj0263; -.
DR PaxDb; 192222-Cj0263; -.
DR EnsemblBacteria; CAL34417; CAL34417; Cj0263.
DR GeneID; 904588; -.
DR KEGG; cje:Cj0263; -.
DR PATRIC; fig|192222.6.peg.257; -.
DR eggNOG; COG0428; Bacteria.
DR HOGENOM; CLU_015114_1_3_7; -.
DR OrthoDB; 9787346at2; -.
DR Proteomes; UP000000799; 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; 2.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion transport; Iron; Membrane;
KW Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc; Zinc transport.
FT CHAIN 1..291
FT /note="Zinc transporter ZupT"
FT /id="PRO_0000207267"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 39..59
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 74..94
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 174..194
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 209..229
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 233..253
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 158
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /note="M2 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 161
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /note="M2 metal binding site"
FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00548"
FT BINDING 186
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /note="M1 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 187
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /note="M2 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 190
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /note="M2 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 190
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /note="M1 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 219
FT /ligand="Fe(2+)"
FT /ligand_id="ChEBI:CHEBI:29033"
FT /note="M2 metal binding site"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
SQ SEQUENCE 291 AA; 31462 MW; 35A0E51E408E1CF2 CRC64;
MQFTFEQIFI AMLLTLFAGF STAIGSIIAF FSRKDDLRVL SLGLGFSAGV MIYISFMEIL
PTALKDFKNH YDSHWAELLG LACFFGGILI SLLIDKLIPE DVNPHEPKED LSELKICPLP
QKGQNPPKFH PGEKLHQINT KALKRTGIFT ALAIAIHNFP EGFATFISSL DNLTLGIAIA
IAVAIHNIPE GLAVSLPIYH ATGDKKKAFI YSALSGFAEP LGAFVGALIL LPFIGDLTLA
ISFAVIAGIM VFISLDELLP AAKTYDKAHD SLYGLIAGMA IMALSLNLLG Q
//