ZNTB_SALTY
ID ZNTB_SALTY Reviewed; 327 AA.
AC Q9EYX5; Q7CQH1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
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:12142406};
GN OrderedLocusNames=STM1656;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 14028s / SGSG 2262;
RX PubMed=12142406; DOI=10.1128/jb.184.16.4369-4373.2002;
RA Worlock A.J., Smith R.L.;
RT "ZntB is a novel Zn(2+) transporter in Salmonella enterica serovar
RT Typhimurium.";
RL J. Bacteriol. 184:4369-4373(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [3]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=12486076; DOI=10.1128/jb.185.1.374-376.2003;
RA Caldwell A.M., Smith R.L.;
RT "Membrane topology of the ZntB efflux system of Salmonella enterica serovar
RT Typhimurium.";
RL J. Bacteriol. 185:374-376(2003).
RN [4] {ECO:0007744|PDB:3NVO, ECO:0007744|PDB:3NWI}
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-262 IN COMPLEX WITH ZINC,
RP SUBUNIT, DOMAIN, AND MUTAGENESIS OF CYS-92; CYS-244 AND CYS-307.
RX PubMed=21565704; DOI=10.1016/j.str.2011.02.011;
RA Wan Q., Ahmad M.F., Fairman J., Gorzelle B., de la Fuente M., Dealwis C.,
RA Maguire M.E.;
RT "X-ray crystallography and isothermal titration calorimetry studies of the
RT Salmonella zinc transporter ZntB.";
RL Structure 19:700-710(2011).
CC -!- FUNCTION: Zinc transporter (PubMed:12142406). Acts as a Zn(2+):proton
CC symporter, which likely mediates zinc ion uptake (By similarity).
CC {ECO:0000250|UniProtKB:P64423, ECO:0000269|PubMed:12142406}.
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 PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:71196;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01565};
CC -!- SUBUNIT: Homopentamer (PubMed:21565704). Can assemble pentamers in the
CC absence of the transmembrane regions (PubMed:21565704).
CC {ECO:0000269|PubMed:21565704}.
CC -!- INTERACTION:
CC Q9EYX5; Q9EYX5: zntB; NbExp=2; IntAct=EBI-15926489, EBI-15926489;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01565, ECO:0000269|PubMed:12486076}; Multi-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_01565, ECO:0000269|PubMed:12486076}.
CC -!- DOMAIN: Forms a funnel-like structure. Contains three Zn(2+) binding
CC sites, two of which could be involved in Zn(2+) transport.
CC {ECO:0000269|PubMed:21565704}.
CC -!- DISRUPTION PHENOTYPE: Disruption of the gene has a marked effect on
CC resistance levels to zinc and cadmium, but does not significantly alter
CC the sensitivities to cobalt, nickel or manganese.
CC {ECO:0000269|PubMed:12142406}.
CC -!- MISCELLANEOUS: A role in zinc efflux has been proposed by Worlock et
CC al, but ZntB was later shown in E.coli to likely mediate zinc uptake,
CC using a transport mechanism that does not resemble the one proposed for
CC homologous CorA channels. {ECO:0000305}.
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; AF308568; AAG40855.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20574.1; -; Genomic_DNA.
DR RefSeq; NP_460615.1; NC_003197.2.
DR RefSeq; WP_000387373.1; NC_003197.2.
DR PDB; 3NVO; X-ray; 2.30 A; A/B=1-262.
DR PDB; 3NWI; X-ray; 3.13 A; A/B/C/D/E=1-262.
DR PDBsum; 3NVO; -.
DR PDBsum; 3NWI; -.
DR AlphaFoldDB; Q9EYX5; -.
DR SMR; Q9EYX5; -.
DR DIP; DIP-59134N; -.
DR STRING; 99287.STM1656; -.
DR TCDB; 1.A.35.4.1; the cora metal ion transporter (mit) family.
DR PaxDb; Q9EYX5; -.
DR EnsemblBacteria; AAL20574; AAL20574; STM1656.
DR GeneID; 1253174; -.
DR KEGG; stm:STM1656; -.
DR PATRIC; fig|99287.12.peg.1750; -.
DR HOGENOM; CLU_007127_2_0_6; -.
DR OMA; MVSVRIF; -.
DR PhylomeDB; Q9EYX5; -.
DR BioCyc; SENT99287:STM1656-MON; -.
DR EvolutionaryTrace; Q9EYX5; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0042802; F:identical protein binding; IPI:IntAct.
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:0005385; F:zinc ion transmembrane transporter activity; IEA:InterPro.
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 Metal-binding; Reference proteome; Transmembrane; Transmembrane helix;
KW Transport; Zinc.
FT CHAIN 1..327
FT /note="Zinc transport protein ZntB"
FT /id="PRO_0000239247"
FT TOPO_DOM 1..273
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01565,
FT ECO:0000269|PubMed:12486076"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01565"
FT TOPO_DOM 295..300
FT /note="Periplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01565,
FT ECO:0000269|PubMed:12486076"
FT TRANSMEM 301..321
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01565"
FT TOPO_DOM 322..327
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01565,
FT ECO:0000269|PubMed:12486076"
FT BINDING 92
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21565704,
FT ECO:0007744|PDB:3NWI"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:21565704,
FT ECO:0007744|PDB:3NWI"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565704,
FT ECO:0007744|PDB:3NWI"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:21565704,
FT ECO:0007744|PDB:3NWI"
FT BINDING 307
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:21565704"
FT MUTAGEN 92
FT /note="C->S: Contains only two zinc binding sites."
FT /evidence="ECO:0000269|PubMed:21565704"
FT MUTAGEN 244
FT /note="C->S: Contains three zinc binding sites, but the
FT third site shows a decreased affinity for zinc."
FT /evidence="ECO:0000269|PubMed:21565704"
FT MUTAGEN 307
FT /note="C->S: Contains only two zinc binding sites."
FT /evidence="ECO:0000269|PubMed:21565704"
FT HELIX 6..9
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 15..20
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 34..39
FT /evidence="ECO:0007829|PDB:3NWI"
FT STRAND 41..46
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 50..58
FT /evidence="ECO:0007829|PDB:3NVO"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 67..70
FT /evidence="ECO:0007829|PDB:3NVO"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:3NWI"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 106..111
FT /evidence="ECO:0007829|PDB:3NVO"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 143..172
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 186..211
FT /evidence="ECO:0007829|PDB:3NVO"
FT HELIX 221..260
FT /evidence="ECO:0007829|PDB:3NVO"
SQ SEQUENCE 327 AA; 36759 MW; A7B30C5FA9CACFF7 CRC64;
MEAIKGSDVN VPDAVFAWLL DGRGGVKPLE DNDVIDSQHP CWLHLNYTHP DSARWLASTP
LLPNNVRDAL AGESSRPRVS RMGEGTLITL RCINGSTDER PDQLVAMRLY MDERFIVSTR
QRKVLALDDV VSDLQEGTGP VDCGGWLVDV CDALTDHASE FIEELHDKII DLEDNLLDQQ
IPPRGFLALL RKQLIVMRRY MAPQRDVYAR LASERLPWMS DDHRRRMQDI ADRLGRGLDE
IDACIARTGI MADEIAQVMQ ESLARRTYTM SLMAMVFLPS TFLTGLFGVN LGGIPGGGWR
FGFSLFCILL VVLIGGVTLW LHRSKWL
