ZNTB_ECOLI
ID ZNTB_ECOLI Reviewed; 327 AA.
AC P64423; P76054; Q2MBF0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Zinc transport protein ZntB {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000305};
GN Name=zntB {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000303|PubMed:29101379};
GN Synonyms=ydaN; OrderedLocusNames=b1342, JW1336;
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [4] {ECO:0007744|PDB:5N9Y}
RP STRUCTURE BY ELECTRON MICROSCOPY (4.20 ANGSTROMS), FUNCTION, CATALYTIC
RP ACTIVITY, SUBUNIT, SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=29101379; DOI=10.1038/s41467-017-01483-7;
RA Gati C., Stetsenko A., Slotboom D.J., Scheres S.H.W., Guskov A.;
RT "The structural basis of proton driven zinc transport by ZntB.";
RL Nat. Commun. 8:1313-1313(2017).
CC -!- FUNCTION: Zinc transporter (PubMed:29101379). Acts as a Zn(2+):proton
CC symporter, which likely mediates zinc ion uptake (PubMed:29101379).
CC Purified ZntB reconstituted in liposomes also binds and transports
CC Cd(2+), Ni(2+) and Co(2+) (PubMed:29101379).
CC {ECO:0000269|PubMed:29101379}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + Zn(2+)(out) = H(+)(in) + Zn(2+)(in);
CC Xref=Rhea:RHEA:71195, ChEBI:CHEBI:15378, ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01565,
CC ECO:0000269|PubMed:29101379};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71196;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01565,
CC ECO:0000305|PubMed:29101379};
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:29101379}.
CC -!- INTERACTION:
CC P64423; P60785: lepA; NbExp=4; IntAct=EBI-553267, EBI-544544;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01565, ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:29101379}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000269|PubMed:29101379}.
CC -!- MISCELLANEOUS: Uses a transport mechanism that does not resemble the
CC one proposed for homologous CorA channels.
CC {ECO:0000269|PubMed:29101379}.
CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) (TC 1.A.35)
CC family. {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000305}.
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DR EMBL; U00096; AAC74424.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76406.1; -; Genomic_DNA.
DR PIR; A64884; A64884.
DR RefSeq; NP_415858.1; NC_000913.3.
DR RefSeq; WP_000387388.1; NZ_SSZK01000012.1.
DR PDB; 5N9Y; EM; 4.20 A; A/B/C/D/E=1-327.
DR PDBsum; 5N9Y; -.
DR AlphaFoldDB; P64423; -.
DR SMR; P64423; -.
DR BioGRID; 4261064; 18.
DR BioGRID; 850275; 2.
DR DIP; DIP-48038N; -.
DR IntAct; P64423; 1.
DR STRING; 511145.b1342; -.
DR jPOST; P64423; -.
DR PaxDb; P64423; -.
DR PRIDE; P64423; -.
DR EnsemblBacteria; AAC74424; AAC74424; b1342.
DR EnsemblBacteria; BAE76406; BAE76406; BAE76406.
DR GeneID; 66674830; -.
DR GeneID; 945910; -.
DR KEGG; ecj:JW1336; -.
DR KEGG; eco:b1342; -.
DR PATRIC; fig|1411691.4.peg.935; -.
DR EchoBASE; EB3139; -.
DR eggNOG; COG0598; Bacteria.
DR HOGENOM; CLU_007127_2_0_6; -.
DR InParanoid; P64423; -.
DR OMA; MVSVRIF; -.
DR PhylomeDB; P64423; -.
DR BioCyc; EcoCyc:G6674-MON; -.
DR BioCyc; MetaCyc:G6674-MON; -.
DR PRO; PR:P64423; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IDA:EcoCyc.
DR GO; GO:0050897; F:cobalt ion binding; IBA:GO_Central.
DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0022883; F:zinc efflux transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0071578; P:zinc ion import across plasma membrane; IDA:EcoCyc.
DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:EcoCyc.
DR HAMAP; MF_01565; ZntB; 1.
DR InterPro; IPR045861; CorA_cytoplasmic_dom.
DR InterPro; IPR045863; CorA_TM1_TM2.
DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB.
DR InterPro; IPR023714; Zn_transp_ZntB.
DR Pfam; PF01544; CorA; 1.
DR SUPFAM; SSF143865; SSF143865; 1.
DR SUPFAM; SSF144083; SSF144083; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport; Zinc.
FT CHAIN 1..327
FT /note="Zinc transport protein ZntB"
FT /id="PRO_0000201315"
FT TOPO_DOM 1..272
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:29101379,
FT ECO:0007744|PDB:5N9Y"
FT TRANSMEM 273..288
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29101379,
FT ECO:0007744|PDB:5N9Y"
FT TOPO_DOM 289..302
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:29101379,
FT ECO:0007744|PDB:5N9Y"
FT TRANSMEM 303..320
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:29101379,
FT ECO:0007744|PDB:5N9Y"
FT TOPO_DOM 321..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:29101379, ECO:0007744|PDB:5N9Y"
SQ SEQUENCE 327 AA; 36612 MW; B3A83F420565775D CRC64;
MEAIKGSDVN VPDAVFAWML DGRGGVKPLE NTDVIDEAHP CWLHLNYVHH DSAQWLATTP
LLPNNVRDAL AGESTRPRVS RLGEGTLITL RCINGSTDER PDQLVAMRVY MDGRLIVSTR
QRKVLALDDV VSDLEEGTGP TDCGGWLVDV CDALTDHSSE FIEQLHDKII DLEDNLLDQQ
IPPRGFLALL RKQLIVMRRY MAPQRDVYAR LASERLPWMS DDQRRRMQDI ADRLGRGLDE
IDACIARTGV MADEIAQVMQ ENLARRTYTM SLMAMVFLPS TFLTGLFGVN LGGIPGGGWQ
FGFSIFCILL VVLIGGVALW LHRSKWL
