A0A0H3LM39 · ZIP_BORBR
- ProteinZinc transporter ZIPB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids309 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Selective electrodiffusional channel that mediates the uptake of Zn2+. Exploits in vivo zinc concentration gradients (maintained by cellular zinc homeostasis) to passively move zinc ions into the cytoplasm. ZIPB-mediated zinc flux is dependent upon pH, but independent of the proton motive force. Is also able to import Cd2+, but is not permeable to Co2+, Cu2+, Fe2+, Mn2+ and Ni2+.
Miscellaneous
The zinc flux through ZIPB is extremely slow in comparison with typical ion channels and is nonsaturating with respect to a zinc concentration up to 2 mM.
Catalytic activity
- Zn2+(in) = Zn2+(out)
- Cd2+(in) = Cd2+(out)
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 89 | Zn2+ 5 (UniProtKB | ChEBI); M7 metal binding site | ||||
Sequence: D | ||||||
Binding site | 99 | Cd2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: M | ||||||
Binding site | 144 | Cd2+ 3 (UniProtKB | ChEBI); M3 metal binding site | ||||
Sequence: D | ||||||
Binding site | 144 | Zn2+ 3 (UniProtKB | ChEBI); M3 metal binding site | ||||
Sequence: D | ||||||
Binding site | 144 | Zn2+ 4 (UniProtKB | ChEBI); M6 metal binding site | ||||
Sequence: D | ||||||
Binding site | 177 | Cd2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: H | ||||||
Binding site | 177 | Zn2+ 2 (UniProtKB | ChEBI); M5 metal binding site | ||||
Sequence: H | ||||||
Binding site | 178 | Cd2+ 2 (UniProtKB | ChEBI); M2 metal binding site | ||||
Sequence: N | ||||||
Binding site | 181 | Cd2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: E | ||||||
Binding site | 181 | Cd2+ 2 (UniProtKB | ChEBI); M2 metal binding site | ||||
Sequence: E | ||||||
Binding site | 181 | Zn2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: E | ||||||
Binding site | 207 | Cd2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: Q | ||||||
Binding site | 207 | Zn2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: Q | ||||||
Binding site | 208 | Cd2+ 2 (UniProtKB | ChEBI); M2 metal binding site | ||||
Sequence: D | ||||||
Binding site | 211 | Cd2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: E | ||||||
Binding site | 211 | Cd2+ 2 (UniProtKB | ChEBI); M2 metal binding site | ||||
Sequence: E | ||||||
Binding site | 211 | Zn2+ 1 (UniProtKB | ChEBI); M1 metal binding site | ||||
Sequence: E | ||||||
Binding site | 240 | Cd2+ 2 (UniProtKB | ChEBI); M2 metal binding site | ||||
Sequence: E | ||||||
Binding site | 275 | Cd2+ 3 (UniProtKB | ChEBI); M3 metal binding site | ||||
Sequence: H | ||||||
Binding site | 275 | Zn2+ 3 (UniProtKB | ChEBI); M3 metal binding site | ||||
Sequence: H | ||||||
Binding site | 276 | Zn2+ 2 (UniProtKB | ChEBI); M5 metal binding site | ||||
Sequence: E | ||||||
Binding site | 286 | Zn2+ 5 (UniProtKB | ChEBI); M7 metal binding site | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | metal ion transmembrane transporter activity | |
Biological Process | zinc ion transport |
Keywords
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameZinc transporter ZIPB
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Betaproteobacteria > Burkholderiales > Alcaligenaceae > Bordetella
Accessions
- Primary accessionA0A0H3LM39
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Cell inner membrane ; Multi-pass membrane protein
Features
Showing features for topological domain, transmembrane.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Topological domain | 1-22 | Periplasmic | ||||
Sequence: MNQPSSLAADLRGAWHAQAQSH | ||||||
Transmembrane | 23-50 | Helical | ||||
Sequence: PLITLGLAASAAGVVLLLVAGIVNALTG | ||||||
Topological domain | 51-55 | Extracellular | ||||
Sequence: ENRVH | ||||||
Transmembrane | 56-81 | Helical | ||||
Sequence: VGYAVLGGAAGFAATALGALMALGLR | ||||||
Topological domain | 82-83 | Periplasmic | ||||
Sequence: AI | ||||||
Transmembrane | 84-119 | Helical | ||||
Sequence: SARTQDAMLGFAAGMMLAASAFSLILPGLDAAGTIV | ||||||
Topological domain | 120-121 | Extracellular | ||||
Sequence: GP | ||||||
Transmembrane | 122-145 | Helical | ||||
Sequence: GPAAAAVVALGLGLGVLLMLGLDY | ||||||
Topological domain | 146-165 | Periplasmic | ||||
Sequence: FTPHEHERTGHQGPEAARVN | ||||||
Transmembrane | 166-190 | Helical | ||||
Sequence: RVWLFVLTIILHNLPEGMAIGVSFA | ||||||
Topological domain | 191-192 | Extracellular | ||||
Sequence: TG | ||||||
Transmembrane | 193-222 | Helical | ||||
Sequence: DLRIGLPLTSAIAIQDVPEGLAVALALRAV | ||||||
Topological domain | 223-224 | Periplasmic | ||||
Sequence: GL | ||||||
Transmembrane | 225-251 | Helical | ||||
Sequence: PIGRAVLVAVASGLMEPLGALVGVGIS | ||||||
Topological domain | 252-255 | Extracellular | ||||
Sequence: SGFA | ||||||
Transmembrane | 256-275 | Helical | ||||
Sequence: LAYPISMGLAAGAMIFVVSH | ||||||
Topological domain | 276-287 | Periplasmic | ||||
Sequence: EVIPETHRNGHE | ||||||
Transmembrane | 288-308 | Helical | ||||
Sequence: TTATVGLMAGFALMMFLDTAL | ||||||
Topological domain | 309 | Extracellular | ||||
Sequence: G |
Keywords
- Cellular component
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 106 | Is more tolerant to high Zn2+ or Cd2+ concentrations due to a decreased metal uptake ability. | ||||
Sequence: S → A | ||||||
Mutagenesis | 144 | Is more tolerant to high Zn2+ or Cd2+ concentrations due to a decreased metal uptake ability. | ||||
Sequence: D → A | ||||||
Mutagenesis | 178 | Loses metal binding at M2 but does not lead to significant changes in either overall structure or metal coordination at M1; when associated with A-208 and A-240. | ||||
Sequence: N → A | ||||||
Mutagenesis | 208 | Loses metal binding at M2 but does not lead to significant changes in either overall structure or metal coordination at M1; when associated with A-178 and A-240. | ||||
Sequence: D → A | ||||||
Mutagenesis | 240 | Loses metal binding at M2 but does not lead to significant changes in either overall structure or metal coordination at M1; when associated with A-178 and A-208. | ||||
Sequence: E → A | ||||||
Mutagenesis | 276 | Is more tolerant to high Zn2+ or Cd2+ concentrations due to a decreased metal uptake ability. | ||||
Sequence: E → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000458195 | 1-309 | Zinc transporter ZIPB | |||
Sequence: MNQPSSLAADLRGAWHAQAQSHPLITLGLAASAAGVVLLLVAGIVNALTGENRVHVGYAVLGGAAGFAATALGALMALGLRAISARTQDAMLGFAAGMMLAASAFSLILPGLDAAGTIVGPGPAAAAVVALGLGLGVLLMLGLDYFTPHEHERTGHQGPEAARVNRVWLFVLTIILHNLPEGMAIGVSFATGDLRIGLPLTSAIAIQDVPEGLAVALALRAVGLPIGRAVLVAVASGLMEPLGALVGVGISSGFALAYPISMGLAAGAMIFVVSHEVIPETHRNGHETTATVGLMAGFALMMFLDTALG |
Structure
Family & Domains
Domain
Has an additional transmembrane segment in the N-terminus compared to many other ZIP family members. This extra helix is important for activity in vivo.
The two metal binding sites M1 and M2 that are halfway through the membrane form a binuclear metal center. The multiple conserved zinc-binding sites (M1,M5, M6 and M3) appear to constitute a route of zinc release to the cytoplasm (PubMed:28875161).
M1 is the primary transport site essential for activity, whereas M2 plays an auxiliary role presumably by serving as an additional transport site and modulating the properties of the primary transport site (PubMed:31914589).
Cd2+ at M1 can readily be replaced by externally added Zn2+, whereas Cd2+ at M2 cannot (PubMed:28875161, PubMed:31914589).
ZIP proteins seem to operate via a two-domain elevator-type mechanism for zinc transport (Probable)
M1 is the primary transport site essential for activity, whereas M2 plays an auxiliary role presumably by serving as an additional transport site and modulating the properties of the primary transport site (PubMed:31914589).
Cd2+ at M1 can readily be replaced by externally added Zn2+, whereas Cd2+ at M2 cannot (PubMed:28875161, PubMed:31914589).
ZIP proteins seem to operate via a two-domain elevator-type mechanism for zinc transport (Probable)
Sequence similarities
Belongs to the ZIP transporter (TC 2.A.5) family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length309
- Mass (Da)30,988
- Last updated2015-09-16 v1
- Checksum9ADF2E45AA8FE5AF
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX640444 EMBL· GenBank· DDBJ | CAE32899.1 EMBL· GenBank· DDBJ | Genomic DNA |