ZINT_ECOLI
ID ZINT_ECOLI Reviewed; 216 AA.
AC P76344; Q2MAZ5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Metal-binding protein ZinT;
DE AltName: Full=Cadmium-induced protein ZinT;
DE Flags: Precursor;
GN Name=zinT; Synonyms=yodA; OrderedLocusNames=b1973, JW1956;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PROTEIN SEQUENCE OF 24-33.
RX PubMed=9579078; DOI=10.1099/00221287-144-4-1045;
RA Ferianc P., Farewell A., Nystroem T.;
RT "The cadmium-stress stimulon of Escherichia coli K-12.";
RL Microbiology 144:1045-1050(1998).
RN [4]
RP INDUCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12480884; DOI=10.1099/00221287-148-12-3801;
RA Puskarova A., Ferianc P., Kormanec J., Homerova D., Farewell A.,
RA Nystroem T.;
RT "Regulation of yodA encoding a novel cadmium-induced protein in Escherichia
RT coli.";
RL Microbiology 148:3801-3811(2002).
RN [5]
RP FUNCTION, METAL-BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=17931600; DOI=10.1016/j.bbrc.2007.09.094;
RA Kershaw C.J., Brown N.L., Hobman J.L.;
RT "Zinc dependence of zinT (yodA) mutants and binding of zinc, cadmium and
RT mercury by ZinT.";
RL Biochem. Biophys. Res. Commun. 364:66-71(2007).
RN [6]
RP CADMIUM-BINDING, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=17632755; DOI=10.1007/s00284-006-0516-5;
RA Stojnev T., Harichova J., Ferianc P., Nystrom T.;
RT "Function of a novel cadmium-induced yodA protein in Escherichia coli.";
RL Curr. Microbiol. 55:99-104(2007).
RN [7]
RP FUNCTION, INDUCTION, DISRUPTION PHENOTYPE, ZINC-BINDING, AND
RP CADMIUM-BINDING.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=19377097; DOI=10.1074/jbc.m109.001503;
RA Graham A.I., Hunt S., Stokes S.L., Bramall N., Bunch J., Cox A.G.,
RA McLeod C.W., Poole R.K.;
RT "Severe zinc depletion of Escherichia coli: roles for high affinity zinc
RT binding by ZinT, zinc transport and zinc-independent proteins.";
RL J. Biol. Chem. 284:18377-18389(2009).
RN [8]
RP INDUCTION.
RC STRAIN=BW21135;
RX PubMed=22196016; DOI=10.1016/j.jinorgbio.2011.11.022;
RA Hensley M.P., Gunasekera T.S., Easton J.A., Sigdel T.K., Sugarbaker S.A.,
RA Klingbeil L., Breece R.M., Tierney D.L., Crowder M.W.;
RT "Characterization of Zn(II)-responsive ribosomal proteins YkgM and L31 in
RT E. coli.";
RL J. Inorg. Biochem. 111:164-172(2012).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 24-216 IN COMPLEX WITH ZINC;
RP CADMIUM AND NICKEL.
RX PubMed=12909634; DOI=10.1074/jbc.m304484200;
RA David G., Blondeau K., Schiltz M., Penel S., Lewit-Bentley A.;
RT "YodA from Escherichia coli is a metal-binding, lipocalin-like protein.";
RL J. Biol. Chem. 278:43728-43735(2003).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.17 ANGSTROMS) IN COMPLEX WITH ZINC.
RG Berkeley structural genomics center (BSGC);
RT "Crystal structure of refined tetragonal crystal of YodA from Escherichia
RT coli.";
RL Submitted (FEB-2009) to the PDB data bank.
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 2-216 IN COMPLEX WITH ZINC.
RG New York structural genomix research consortium (NYSGXRC);
RT "Crystal structure of a hypothetical protein YodA.";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: May function as a periplasmic zinc chaperone or mediate
CC direct transport of zinc from the periplasm to the cytoplasm under
CC zinc-limited conditions. Binds zinc with high affinity, and can also
CC bind cadmium, mercury or nickel. Preferentially binds Zn(2+) over
CC Cd(2+). Contains one high affinity metal binding site, and can bind
CC additional metal ions at other sites. {ECO:0000269|PubMed:17931600,
CC ECO:0000269|PubMed:19377097}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12480884}.
CC Periplasm {ECO:0000269|PubMed:12480884}. Note=Cytoplasmic in
CC nonstressed cells, and exported to the periplasm upon exposure to
CC cadmium.
CC -!- INDUCTION: Repressed by Zur. Up-regulated in response to extreme Zn(2+)
CC deprivation. Also induced by cadmium and hydrogen peroxide.
CC {ECO:0000269|PubMed:12480884, ECO:0000269|PubMed:19377097,
CC ECO:0000269|PubMed:22196016}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows a growth defect and a lowered
CC cellular Zn(2+) level under Zn(2+) limitation. Mutant does not bind
CC cadmium. {ECO:0000269|PubMed:17632755, ECO:0000269|PubMed:17931600,
CC ECO:0000269|PubMed:19377097}.
CC -!- SIMILARITY: Belongs to the calycin superfamily. ZinT family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U00096; AAC75039.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76561.1; -; Genomic_DNA.
DR PIR; A64962; A64962.
DR RefSeq; NP_416482.1; NC_000913.3.
DR RefSeq; WP_001007805.1; NZ_LN832404.1.
DR PDB; 1OEE; X-ray; 2.10 A; A=24-216.
DR PDB; 1OEJ; X-ray; 1.81 A; A=24-216.
DR PDB; 1OEK; X-ray; 2.40 A; A=24-216.
DR PDB; 1S7D; X-ray; 2.17 A; A=1-216.
DR PDB; 1TXL; X-ray; 1.70 A; A=2-216.
DR PDB; 5AQ6; X-ray; 1.79 A; A=24-216.
DR PDB; 5XM5; X-ray; 1.49 A; A/B=24-216.
DR PDB; 5YXC; X-ray; 1.76 A; A/B=1-216.
DR PDB; 6LM2; X-ray; 2.13 A; A=32-215.
DR PDBsum; 1OEE; -.
DR PDBsum; 1OEJ; -.
DR PDBsum; 1OEK; -.
DR PDBsum; 1S7D; -.
DR PDBsum; 1TXL; -.
DR PDBsum; 5AQ6; -.
DR PDBsum; 5XM5; -.
DR PDBsum; 5YXC; -.
DR PDBsum; 6LM2; -.
DR AlphaFoldDB; P76344; -.
DR SMR; P76344; -.
DR BioGRID; 4260387; 38.
DR BioGRID; 850831; 14.
DR IntAct; P76344; 16.
DR STRING; 511145.b1973; -.
DR SWISS-2DPAGE; P76344; -.
DR PaxDb; P76344; -.
DR PRIDE; P76344; -.
DR DNASU; 946480; -.
DR EnsemblBacteria; AAC75039; AAC75039; b1973.
DR EnsemblBacteria; BAE76561; BAE76561; BAE76561.
DR GeneID; 66674137; -.
DR GeneID; 946480; -.
DR KEGG; ecj:JW1956; -.
DR KEGG; eco:b1973; -.
DR PATRIC; fig|1411691.4.peg.277; -.
DR EchoBASE; EB3802; -.
DR eggNOG; COG3443; Bacteria.
DR HOGENOM; CLU_072001_1_0_6; -.
DR InParanoid; P76344; -.
DR OMA; MGNTSHE; -.
DR PhylomeDB; P76344; -.
DR BioCyc; EcoCyc:G7061-MON; -.
DR EvolutionaryTrace; P76344; -.
DR PRO; PR:P76344; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:0046870; F:cadmium ion binding; IDA:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0071276; P:cellular response to cadmium ion; IEP:EcoCyc.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IEP:EcoCyc.
DR GO; GO:0034224; P:cellular response to zinc ion starvation; IEP:EcoCyc.
DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:EcoCyc.
DR Gene3D; 2.40.128.20; -; 1.
DR InterPro; IPR012674; Calycin.
DR InterPro; IPR015304; ZinT_dom.
DR Pfam; PF09223; ZinT; 1.
DR SUPFAM; SSF50814; SSF50814; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cadmium; Cytoplasm; Direct protein sequencing; Metal-binding;
KW Nickel; Periplasm; Reference proteome; Signal; Zinc.
FT SIGNAL 1..23
FT /evidence="ECO:0000269|PubMed:9579078"
FT CHAIN 24..216
FT /note="Metal-binding protein ZinT"
FT /id="PRO_0000013865"
FT BINDING 167
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT BINDING 178
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT BINDING 212
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12909634, ECO:0000269|Ref.10,
FT ECO:0000269|Ref.11"
FT HELIX 35..41
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 55..58
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 66..70
FT /evidence="ECO:0007829|PDB:5XM5"
FT TURN 71..74
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 75..84
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 90..101
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 114..119
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 122..127
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 175..184
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5XM5"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:5XM5"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:5XM5"
SQ SEQUENCE 216 AA; 24762 MW; EBEE9DC73513B9C2 CRC64;
MAIRLYKLAV ALGVFIVSAP AFSHGHHSHG KPLTEVEQKA ANGVFDDANV QNRTLSDWDG
VWQSVYPLLQ SGKLDPVFQK KADADKTKTF AEIKDYYHKG YATDIEMIGI EDGIVEFHRN
NETTSCKYDY DGYKILTYKS GKKGVRYLFE CKDPESKAPK YIQFSDHIIA PRKSSHFHIF
MGNDSQQSLL NEMENWPTYY PYQLSSEEVV EEMMSH
