P0AFJ7 · PITA_ECOLI
- ProteinLow-affinity inorganic phosphate transporter PitA
- GenepitA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids499 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Low-affinity inorganic phosphate transporter (PubMed:11489853, PubMed:328484, PubMed:6998957, PubMed:8110778).
Mediates proton-driven uptake of soluble neutral metal phosphate (MeHP04) complexes (PubMed:8110778).
It can use Mg2+, Ca2+, Co2+ and Mn2+ (PubMed:8110778).
Activity impacts bacterial growth in low Mg2+ conditions (PubMed:30276893).
Is also involved in Zn2+ uptake, probably via formation of a ZnHPO4 complex (PubMed:10713426).
Can also transport arsenate (PubMed:328484). Involved in the uptake of tellurite (PubMed:23189244).
Mediates proton-driven uptake of soluble neutral metal phosphate (MeHP04) complexes (PubMed:8110778).
It can use Mg2+, Ca2+, Co2+ and Mn2+ (PubMed:8110778).
Activity impacts bacterial growth in low Mg2+ conditions (PubMed:30276893).
Is also involved in Zn2+ uptake, probably via formation of a ZnHPO4 complex (PubMed:10713426).
Can also transport arsenate (PubMed:328484). Involved in the uptake of tellurite (PubMed:23189244).
Miscellaneous
The Pit system in E.coli K12 consists of two transporters, PitA and PitB, which can transport phosphate independently of each other. Both proteins may have contributed to the kinetic values and substrate specificities determined in earlier studies.
Catalytic activity
- phosphate(in) + H+(in) = phosphate(out) + H+(out)phosphate (in)CHEBI:43474
+ H+ (in)CHEBI:15378= phosphate (out)CHEBI:43474+ H+ (out)CHEBI:15378 - arsenate(in) + H+(in) = arsenate(out) + H+(out)
Activity regulation
Phosphate uptake is dependent on the presence of divalent cations, which form soluble metal phosphate (MeHP04) complexes (PubMed:10713426, PubMed:8110778).
In Mg2+-limiting conditions, the PhoQP-regulated small protein MgtS and sRNA MgrR both regulate the PitA transporter, leading to increased intracellular Mg2+ (PubMed:30276893).
Metal phosphate uptake is inhibited at low internal pH (PubMed:8110778).
Inhibited by the uncoupler carbonyl cyanide m-chlorophenylhydrazone (CCCP) (PubMed:328484). Is also inhibited by the energy uncoupler 2,4-dinitrophenol and the sulfhydryl reagent N-ethylmaleimide (PubMed:6998957).
In Mg2+-limiting conditions, the PhoQP-regulated small protein MgtS and sRNA MgrR both regulate the PitA transporter, leading to increased intracellular Mg2+ (PubMed:30276893).
Metal phosphate uptake is inhibited at low internal pH (PubMed:8110778).
Inhibited by the uncoupler carbonyl cyanide m-chlorophenylhydrazone (CCCP) (PubMed:328484). Is also inhibited by the energy uncoupler 2,4-dinitrophenol and the sulfhydryl reagent N-ethylmaleimide (PubMed:6998957).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
1.9 μM | phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
58 nmol/min/mg | 6.6 | 1.8 mM Mg2+ | |||
39 nmol/min/mg | 7.0 | 10.0 mM Mg2+ |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | plasma membrane | |
Molecular Function | arsenate ion transmembrane transporter activity | |
Molecular Function | phosphate transmembrane transporter activity | |
Molecular Function | solute:proton symporter activity | |
Molecular Function | tellurite transmembrane transporter activity | |
Molecular Function | zinc ion transmembrane transporter activity | |
Biological Process | arsenate ion transmembrane transport | |
Biological Process | magnesium ion homeostasis | |
Biological Process | phosphate ion transmembrane transport | |
Biological Process | tellurite transport |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameLow-affinity inorganic phosphate transporter PitA
- Alternative names
Gene names
Organism names
- Organism
- Strains
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionP0AFJ7
- Secondary accessions
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 | 1-4 | Periplasmic | ||||
Sequence: MLHL | ||||||
Transmembrane | 5-25 | Helical | ||||
Sequence: FAGLDLHTGLLLLLALAFVLF | ||||||
Topological domain | 26-51 | Cytoplasmic | ||||
Sequence: YEAINGFHDTANAVATVIYTRAMRSQ | ||||||
Transmembrane | 52-72 | Helical | ||||
Sequence: LAVVMAAVFNFLGVLLGGLSV | ||||||
Topological domain | 73-93 | Periplasmic | ||||
Sequence: AYAIVHMLPTDLLLNMGSSHG | ||||||
Transmembrane | 94-114 | Helical | ||||
Sequence: LAMVFSMLLAAIIWNLGTWYF | ||||||
Topological domain | 115-123 | Cytoplasmic | ||||
Sequence: GLPASSSHT | ||||||
Transmembrane | 124-144 | Helical | ||||
Sequence: LIGAIIGIGLTNALMTGTSVV | ||||||
Topological domain | 145-154 | Periplasmic | ||||
Sequence: DALNIPKVLS | ||||||
Transmembrane | 155-175 | Helical | ||||
Sequence: IFGSLIVSPIVGLVFAGGLIF | ||||||
Topological domain | 176-206 | Cytoplasmic | ||||
Sequence: LLRRYWSGTKKRARIHLTPAEREKKDGKKKP | ||||||
Transmembrane | 207-227 | Helical | ||||
Sequence: PFWTRIALILSAIGVAFSHGA | ||||||
Topological domain | 228-232 | Periplasmic | ||||
Sequence: NDGQK | ||||||
Transmembrane | 233-253 | Helical | ||||
Sequence: GIGLVMLVLIGVAPAGFVVNM | ||||||
Topological domain | 254-381 | Cytoplasmic | ||||
Sequence: NATGYEITRTRDAINNVEAYFEQHPALLKQATGADQLVPAPEAGATQPAEFHCHPSNTINALNRLKGMLTTDVESYDKLSLDQRSQMRRIMLCVSDTIDKVVKMPGVSADDQRLLKKLKSDMLSTIEY | ||||||
Transmembrane | 382-402 | Helical | ||||
Sequence: APVWIIMAVALALGIGTMIGW | ||||||
Topological domain | 403-429 | Periplasmic | ||||
Sequence: RRVATTIGEKIGKKGMTYAQGMSAQMT | ||||||
Transmembrane | 430-450 | Helical | ||||
Sequence: AAVSIGLASYTGMPVSTTHVL | ||||||
Topological domain | 451-472 | Cytoplasmic | ||||
Sequence: SSSVAGTMVVDGGGLQRKTVTS | ||||||
Transmembrane | 473-493 | Helical | ||||
Sequence: ILMAWVFTLPAAVLLSGGLYW | ||||||
Topological domain | 494-499 | Periplasmic | ||||
Sequence: LSLQFL |
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Disruption of the gene confers increased resistance to Zn2+, associated with reduced accumulation of Zn2+ when cells are exposed to concentrations of ZnSO4 below the minimal inhibitory concentration (MIC) (PubMed:10713426).
Mutant is approximately four-fold more tolerant to tellurite, and cell viability remains almost unchanged during prolonged exposure to the toxicant as compared with wild type (PubMed:23189244).
Mutant is approximately four-fold more tolerant to tellurite, and cell viability remains almost unchanged during prolonged exposure to the toxicant as compared with wild type (PubMed:23189244).
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 220 | Loss of activity. Cannot grow on inorganic phosphate medium. | ||||
Sequence: G → D |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000080782 | 1-499 | Low-affinity inorganic phosphate transporter PitA | |||
Sequence: MLHLFAGLDLHTGLLLLLALAFVLFYEAINGFHDTANAVATVIYTRAMRSQLAVVMAAVFNFLGVLLGGLSVAYAIVHMLPTDLLLNMGSSHGLAMVFSMLLAAIIWNLGTWYFGLPASSSHTLIGAIIGIGLTNALMTGTSVVDALNIPKVLSIFGSLIVSPIVGLVFAGGLIFLLRRYWSGTKKRARIHLTPAEREKKDGKKKPPFWTRIALILSAIGVAFSHGANDGQKGIGLVMLVLIGVAPAGFVVNMNATGYEITRTRDAINNVEAYFEQHPALLKQATGADQLVPAPEAGATQPAEFHCHPSNTINALNRLKGMLTTDVESYDKLSLDQRSQMRRIMLCVSDTIDKVVKMPGVSADDQRLLKKLKSDMLSTIEYAPVWIIMAVALALGIGTMIGWRRVATTIGEKIGKKGMTYAQGMSAQMTAAVSIGLASYTGMPVSTTHVLSSSVAGTMVVDGGGLQRKTVTSILMAWVFTLPAAVLLSGGLYWLSLQFL |
Proteomic databases
Structure
Family & Domains
Sequence similarities
Belongs to the inorganic phosphate transporter (PiT) (TC 2.A.20) family. Pit subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length499
- Mass (Da)53,389
- Last updated2005-12-20 v1
- Checksum93D551131C524084
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
U00039 EMBL· GenBank· DDBJ | AAB18469.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
U00096 EMBL· GenBank· DDBJ | AAC76518.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AP009048 EMBL· GenBank· DDBJ | BAE77801.1 EMBL· GenBank· DDBJ | Genomic DNA |