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Protein

Molybdate-binding protein ModA

Gene

modA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi36MolybdateCombined sources1 Publication1
Metal bindingi63MolybdateCombined sources1 Publication1
Metal bindingi149Molybdate; via amide nitrogenCombined sources1 Publication1
Metal bindingi176Molybdate; via amide nitrogenCombined sources1 Publication1
Metal bindingi194MolybdateCombined sources1 Publication1

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 processChromate resistance, Transport
LigandMetal-binding, Molybdenum, Tungsten

Enzyme and pathway databases

BioCyciEcoCyc:MODA-MONOMER
MetaCyc:MODA-MONOMER

Protein family/group databases

TCDBi3.A.1.8.1 the atp-binding cassette (abc) superfamily

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdate-binding protein ModA3 Publications
Alternative name(s):
Molybdate/tungstate-binding protein ModACurated
Gene namesi
Name:modA
Ordered Locus Names:b0763, JW0746
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG12427 modA

Subcellular locationi

GO - Cellular componenti

  • outer membrane-bounded periplasmic space Source: EcoCyc

Keywords - Cellular componenti

Periplasm

Pathology & 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 keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi35A → 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 Publication1
Mutagenesisi36S → A: Loss of chromate removal from a buffered solution; when associated with A-63. 1 Publication1
Mutagenesisi36S → C: Loss of binding to perrhenate. Slightly reduced chromate removal from a buffered solution. 2 Publications1
Mutagenesisi36S → 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 Publications1
Mutagenesisi36S → E: Slightly reduced chromate removal from a buffered solution. 1 Publication1
Mutagenesisi63S → A: Loss of chromate removal from a buffered solution; when associated with A-36. 1 Publication1
Mutagenesisi63S → C: Reduced binding affinity for perrhenate. 1 Publication1
Mutagenesisi63S → D: Reduced binding affinity for perrhenate. Significantly reduced chromate removal from a buffered solution; when associated with D-36. 2 Publications1
Mutagenesisi175D → N: Reduced binding affinity for perrhenate. 1 Publication1
Mutagenesisi177R → 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 Publication1
Mutagenesisi199V → A, Y or W: No change in affinity for perrhenate. 1 Publication1
Mutagenesisi218V → A, Y or W: No change in affinity for perrhenate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 241 PublicationAdd BLAST24
ChainiPRO_000003182725 – 257Molybdate-binding protein ModAAdd BLAST233

Proteomic databases

PaxDbiP37329
PRIDEiP37329

2D gel databases

SWISS-2DPAGEiP37329

Expressioni

Inductioni

Expression is up-regulated by molybdate limitation (PubMed:7860583). Repressed by molybdate-bound ModE (PubMed:8550508).2 Publications

Interactioni

Subunit structurei

The complex is composed of two ATP-binding proteins (ModC), two transmembrane proteins (ModB) and a solute-binding protein (ModA).Curated

Protein-protein interaction databases

BioGridi4262087, 14 interactors
IntActiP37329, 1 interactor
STRINGi316385.ECDH10B_0831

Structurei

Secondary structure

1257
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi29 – 34Combined sources6
Helixi35 – 37Combined sources3
Helixi38 – 52Combined sources15
Beta strandi56 – 61Combined sources6
Helixi63 – 72Combined sources10
Beta strandi77 – 80Combined sources4
Helixi84 – 92Combined sources9
Helixi98 – 100Combined sources3
Beta strandi102 – 107Combined sources6
Beta strandi109 – 114Combined sources6
Helixi130 – 134Combined sources5
Beta strandi139 – 142Combined sources4
Turni144 – 146Combined sources3
Helixi148 – 159Combined sources12
Helixi163 – 166Combined sources4
Helixi167 – 169Combined sources3
Beta strandi170 – 175Combined sources6
Helixi176 – 184Combined sources9
Beta strandi187 – 194Combined sources8
Helixi195 – 200Combined sources6
Beta strandi204 – 209Combined sources6
Helixi212 – 214Combined sources3
Beta strandi218 – 225Combined sources8
Helixi231 – 240Combined sources10
Helixi243 – 251Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AMFX-ray1.75A25-257[»]
1WODX-ray1.75A25-257[»]
3AXFX-ray2.00A/B/C25-257[»]
3R26X-ray1.70A25-257[»]
4XXUX-ray1.43A/B1-257[»]
ProteinModelPortaliP37329
SMRiP37329
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP37329

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4108S6J Bacteria
COG0725 LUCA
HOGENOMiHOG000280537
InParanoidiP37329
KOiK02020
OMAiLTHENLW
PhylomeDBiP37329

Family and domain databases

InterProiView protein in InterPro
IPR005950 ModA
PIRSFiPIRSF004846 ModA, 1 hit
TIGRFAMsiTIGR01256 modA, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P37329-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:257
Mass (Da):27,364
Last modified:October 1, 1994 - v1
Checksum:i847DB740EE0564E7
GO

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
PIRiC64812
RefSeqiNP_415284.1, NC_000913.3
WP_000101984.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73850; AAC73850; b0763
BAA35427; BAA35427; BAA35427
GeneIDi945364
KEGGiecj:JW0746
eco:b0763
PATRICifig|1411691.4.peg.1515

Similar proteinsi

Entry informationi

Entry nameiMODA_ECOLI
AccessioniPrimary (citable) accession number: P37329
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: March 28, 2018
This is version 146 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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