UniProtKB - P37329 (MODA_ECOLI)
Protein
Molybdate-binding protein ModA
Gene
modA
Organism
Escherichia coli (strain K12)
Status
Functioni
Part of the ABC transporter complex ModABC involved in the transport of molybdenum into the cell (PubMed:8576221). Binds molybdate with high affinity in vitro and with a similar affinity in vivo (PubMed:21861186, PubMed:28150901, PubMed:9545596, PubMed:8576221, PubMed:21784948, PubMed:8409926). Binds tungstate with high affinity in vitro (PubMed:28150901, PubMed:9545596, PubMed:8576221, PubMed:21784948). Binds unnatural anion perrhenate with high affinity in vitro (PubMed:21861186). Does not bind sulfate, phosphate, arsenate, selenate, chlorate, metavanadate, nitrate, perchlorate, permanganate or carbonate (PubMed:9545596, PubMed:28150901, PubMed:8576221).6 Publications
Caution
According to a report, does not bind chromate (PubMed:8576221). According to another report, binds chromate with high affinity and is able to remove it from an aqueous solution in vitro (PubMed:28150901).2 Publications
The mod operon containing this protein has previously been called the chlD locus.Curated
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 36 | MolybdateCombined sources1 Publication | 1 | |
Metal bindingi | 63 | MolybdateCombined sources1 Publication | 1 | |
Metal bindingi | 149 | Molybdate; via amide nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 176 | Molybdate; via amide nitrogenCombined sources1 Publication | 1 | |
Metal bindingi | 194 | MolybdateCombined sources1 Publication | 1 |
GO - Molecular functioni
- ATPase-coupled molybdate transmembrane transporter activity Source: UniProtKB
- molybdate ion binding Source: UniProtKB
- molybdenum ion binding Source: EcoCyc
- tungstate binding Source: UniProtKB
GO - Biological processi
- molybdate ion transport Source: EcoCyc
- response to chromate Source: UniProtKB-KW
Keywordsi
Biological process | Chromate resistance, Transport |
Ligand | Metal-binding, Molybdenum, Tungsten |
Enzyme and pathway databases
BioCyci | EcoCyc:MODA-MONOMER MetaCyc:MODA-MONOMER |
Protein family/group databases
TCDBi | 3.A.1.8.1, the atp-binding cassette (abc) superfamily |
Names & Taxonomyi
Protein namesi | Recommended name: Molybdate-binding protein ModA3 PublicationsAlternative name(s): Molybdate/tungstate-binding protein ModACurated |
Gene namesi | Name:modA Ordered Locus Names:b0763, JW0746 |
Organismi | Escherichia coli (strain K12) |
Taxonomic identifieri | 83333 [NCBI] |
Taxonomic lineagei | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacterales › Enterobacteriaceae › Escherichia › |
Proteomesi |
|
Subcellular locationi
- Periplasm 3 Publications
GO - Cellular componenti
- outer membrane-bounded periplasmic space Source: EcoCyc
Keywords - Cellular componenti
PeriplasmPathology & Biotechi
Biotechnological usei
May be useful in radiopharmaceutical applications as an engineered disulfide bond-containing protein with increased affinity for perrhenate (PubMed:21861186). May be used to remove chromate, which is toxic to many biological systems, from environmental aqueous solutions (PubMed:28150901).2 Publications
Disruption phenotypei
Cells are unable to transport molybdate unless high levels of it is supplied in the culture medium.1 Publication
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 35 | A → C: About 5-fold increased binding affinity for perrhenate as a result of formation of an intramolecular disulfide bond with mutant C-177, which stabilizes the metal-bound closed conformation, but no increased binding affinity for molybdate; when associated with C-177. 1 Publication | 1 | |
Mutagenesisi | 36 | S → A: Loss of chromate removal from a buffered solution; when associated with A-63. 1 Publication | 1 | |
Mutagenesisi | 36 | S → C: Loss of binding to perrhenate. Slightly reduced chromate removal from a buffered solution. 2 Publications | 1 | |
Mutagenesisi | 36 | S → D: Loss of binding to perrhenate. Slightly reduced chromate removal from a buffered solution. Significantly reduced chromate removal from a buffered solution; when associated with D-63. 2 Publications | 1 | |
Mutagenesisi | 36 | S → E: Slightly reduced chromate removal from a buffered solution. 1 Publication | 1 | |
Mutagenesisi | 63 | S → A: Loss of chromate removal from a buffered solution; when associated with A-36. 1 Publication | 1 | |
Mutagenesisi | 63 | S → C: Reduced binding affinity for perrhenate. 1 Publication | 1 | |
Mutagenesisi | 63 | S → D: Reduced binding affinity for perrhenate. Significantly reduced chromate removal from a buffered solution; when associated with D-36. 2 Publications | 1 | |
Mutagenesisi | 175 | D → N: Reduced binding affinity for perrhenate. 1 Publication | 1 | |
Mutagenesisi | 177 | R → C: About 5-fold increased binding affinity for perrhenate as a result of formation of an intramolecular disulfide bond with mutant C-35, which stabilizes the metal-bound closed conformation, but no increased binding affinity for molybdate; when associated with C-35. 1 Publication | 1 | |
Mutagenesisi | 199 | V → A, Y or W: No change in affinity for perrhenate. 1 Publication | 1 | |
Mutagenesisi | 218 | V → A, Y or W: No change in affinity for perrhenate. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | 1 PublicationAdd BLAST | 24 | |
ChainiPRO_0000031827 | 25 – 257 | Molybdate-binding protein ModAAdd BLAST | 233 |
Proteomic databases
jPOSTi | P37329 |
PaxDbi | P37329 |
PRIDEi | P37329 |
2D gel databases
SWISS-2DPAGEi | P37329 |
Expressioni
Inductioni
Interactioni
Subunit structurei
The complex is composed of two ATP-binding proteins (ModC), two transmembrane proteins (ModB) and a solute-binding protein (ModA).
CuratedProtein-protein interaction databases
BioGRIDi | 4262087, 14 interactors |
ComplexPortali | CPX-4342, Molybdate ABC transporter complex |
IntActi | P37329, 1 interactor |
STRINGi | 511145.b0763 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P37329 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P37329 |
Family & Domainsi
Sequence similaritiesi
Belongs to the bacterial solute-binding protein ModA family.Curated
Keywords - Domaini
SignalPhylogenomic databases
eggNOGi | COG0725, Bacteria |
HOGENOMi | CLU_065520_3_0_6 |
InParanoidi | P37329 |
PhylomeDBi | P37329 |
Family and domain databases
InterProi | View protein in InterPro IPR005950, ModA |
PIRSFi | PIRSF004846, ModA, 1 hit |
TIGRFAMsi | TIGR01256, modA, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P37329-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MARKWLNLFA GAALSFAVAG NALADEGKIT VFAAASLTNA MQDIATQFKK
60 70 80 90 100
EKGVDVVSSF ASSSTLARQI EAGAPADLFI SADQKWMDYA VDKKAIDTAT
110 120 130 140 150
RQTLLGNSLV VVAPKASVQK DFTIDSKTNW TSLLNGGRLA VGDPEHVPAG
160 170 180 190 200
IYAKEALQKL GAWDTLSPKL APAEDVRGAL ALVERNEAPL GIVYGSDAVA
210 220 230 240 250
SKGVKVVATF PEDSHKKVEY PVAVVEGHNN ATVKAFYDYL KGPQAAEIFK
RYGFTIK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L34009 Genomic DNA Translation: AAB00835.1 U27192 Genomic DNA Translation: AAB60171.1 U07867 Genomic DNA Translation: AAB06893.1 U00096 Genomic DNA Translation: AAC73850.1 AP009048 Genomic DNA Translation: BAA35427.1 |
PIRi | C64812 |
RefSeqi | NP_415284.1, NC_000913.3 WP_000101984.1, NZ_LN832404.1 |
Genome annotation databases
EnsemblBacteriai | AAC73850; AAC73850; b0763 BAA35427; BAA35427; BAA35427 |
GeneIDi | 57728442 945364 |
KEGGi | ecj:JW0746 eco:b0763 |
PATRICi | fig|1411691.4.peg.1515 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L34009 Genomic DNA Translation: AAB00835.1 U27192 Genomic DNA Translation: AAB60171.1 U07867 Genomic DNA Translation: AAB06893.1 U00096 Genomic DNA Translation: AAC73850.1 AP009048 Genomic DNA Translation: BAA35427.1 |
PIRi | C64812 |
RefSeqi | NP_415284.1, NC_000913.3 WP_000101984.1, NZ_LN832404.1 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1AMF | X-ray | 1.75 | A | 25-257 | [»] | |
1WOD | X-ray | 1.75 | A | 25-257 | [»] | |
3AXF | X-ray | 2.00 | A/B/C | 25-257 | [»] | |
3R26 | X-ray | 1.70 | A | 25-257 | [»] | |
4XXU | X-ray | 1.43 | A/B | 1-257 | [»] | |
SMRi | P37329 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 4262087, 14 interactors |
ComplexPortali | CPX-4342, Molybdate ABC transporter complex |
IntActi | P37329, 1 interactor |
STRINGi | 511145.b0763 |
Protein family/group databases
TCDBi | 3.A.1.8.1, the atp-binding cassette (abc) superfamily |
2D gel databases
SWISS-2DPAGEi | P37329 |
Proteomic databases
jPOSTi | P37329 |
PaxDbi | P37329 |
PRIDEi | P37329 |
Genome annotation databases
EnsemblBacteriai | AAC73850; AAC73850; b0763 BAA35427; BAA35427; BAA35427 |
GeneIDi | 57728442 945364 |
KEGGi | ecj:JW0746 eco:b0763 |
PATRICi | fig|1411691.4.peg.1515 |
Organism-specific databases
EchoBASEi | EB2325 |
Phylogenomic databases
eggNOGi | COG0725, Bacteria |
HOGENOMi | CLU_065520_3_0_6 |
InParanoidi | P37329 |
PhylomeDBi | P37329 |
Enzyme and pathway databases
BioCyci | EcoCyc:MODA-MONOMER MetaCyc:MODA-MONOMER |
Miscellaneous databases
EvolutionaryTracei | P37329 |
PROi | PR:P37329 |
Family and domain databases
InterProi | View protein in InterPro IPR005950, ModA |
PIRSFi | PIRSF004846, ModA, 1 hit |
TIGRFAMsi | TIGR01256, modA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MODA_ECOLI | |
Accessioni | P37329Primary (citable) accession number: P37329 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | October 1, 1994 |
Last sequence update: | October 1, 1994 | |
Last modified: | February 10, 2021 | |
This is version 160 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families