ID ZUPT_SALTI Reviewed; 257 AA.
AC P67471; Q8XGR4;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 106.
DE RecName: Full=Zinc transporter ZupT {ECO:0000255|HAMAP-Rule:MF_00548};
GN Name=zupT {ECO:0000255|HAMAP-Rule:MF_00548};
GN OrderedLocusNames=STY3368, t3111;
OS Salmonella typhi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD07716.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO70654.1; -; Genomic_DNA.
DR RefSeq; NP_457582.1; NC_003198.1.
DR RefSeq; WP_000115874.1; NZ_WSUR01000003.1.
DR AlphaFoldDB; P67471; -.
DR SMR; P67471; -.
DR STRING; 220341.gene:17587225; -.
DR KEGG; stt:t3111; -.
DR KEGG; sty:STY3368; -.
DR PATRIC; fig|220341.7.peg.3429; -.
DR eggNOG; COG0428; Bacteria.
DR HOGENOM; CLU_015114_1_3_6; -.
DR OMA; HESTGPC; -.
DR OrthoDB; 9787346at2; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Transmembrane; Transmembrane helix; Transport; Zinc;
KW Zinc transport.
FT CHAIN 1..257
FT /note="Zinc transporter ZupT"
FT /id="PRO_0000207278"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 61..81
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00548"
FT BINDING 120
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 123
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 123
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 148
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 149
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 152
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 152
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 181
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 257 AA; 26544 MW; 268041BBB10139F3 CRC64;
MSVPLILTLL AGAATFIGAF LGVLGQKPSN RVLAFSLGFA AGIMLLISLM EMLPAALDTE
GMSPVLGYGM FIIGLLGYFG LDRLLPHAHP QDLVQKRQQP LPGSIKRTAI LLTLGISLHN
FPEGIATFVT ASSNLELGFG IALAVALHNI PEGLAVAGPV YAATGSKRTA IFWAGISGMA
EILGGVLAWL ILGSLVSPIV MAAIMAAVAG IMVALSVDEL MPLAKEIDPN NNPSYGVLCG
MSIMGLSLVI LQTIGIG
//
