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Database: UniProt
Entry: Q9PIN2
LinkDB: Q9PIN2
Original site: Q9PIN2 
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
//
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