Recombinant Escherichia coli Phosphoenolpyruvate-protein phosphotransferase (ptsI)

Code CSB-YP362529ENV
MSDS
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Source Yeast
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Code CSB-EP362529ENV
MSDS
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Source E.coli
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Code CSB-EP362529ENV-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP362529ENV
MSDS
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Source Baculovirus
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Code CSB-MP362529ENV
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ptsI
Uniprot No.
Alternative Names
ptsI; b2416; JW2409; Phosphoenolpyruvate-protein phosphotransferase; EC 2.7.3.9; Phosphotransferase system; enzyme I
Species
Escherichia coli (strain K12)
Expression Region
1-575
Target Protein Sequence
MISGILASPG IAFGKALLLK EDEIVIDRKK ISADQVDQEV ERFLSGRAKA SAQLETIKTK AGETFGEEKE AIFEGHIMLL EDEELEQEII ALIKDKHMTA DAAAHEVIEG QASALEELDD EYLKERAADV RDIGKRLLRN ILGLKIIDLS AIQDEVILVA ADLTPSETAQ LNLKKVLGFI TDAGGRTSHT SIMARSLELP AIVGTGSVTS QVKNDDYLIL DAVNNQVYVN PTNEVIDKMR AVQEQVASEK AELAKLKDLP AITLDGHQVE VCANIGTVRD VEGAERNGAE GVGLYRTEFL FMDRDALPTE EEQFAAYKAV AEACGSQAVI VRTMDIGGDK ELPYMNFPKE ENPFLGWRAI RIAMDRREIL RDQLRAILRA SAFGKLRIMF PMIISVEEVR ALRKEIEIYK QELRDEGKAF DESIEIGVMV ETPAAATIAR HLAKEVDFFS IGTNDLTQYT LAVDRGNDMI SHLYQPMSPS VLNLIKQVID ASHAEGKWTG MCGELAGDER ATLLLLGMGL DEFSMSAISI PRIKKIIRNT NFEDAKVLAE QALAQPTTDE LMTLVNKFIE EKTIC
Protein Length
full length protein
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfers the phosphoryl group from phosphoenolpyruvate (PEP) to the phosphoryl carrier protein (HPr). Can also use (Z)-3-fluoro-PEP (ZFPEP), (Z)-3-methyl-PEP (ZMePEP), (Z)-3-chloro-PEP (ZClPEP) and (E)-3-chloro-PEP (EClPEP) as alternative phosphoryl donors.
Gene References into Functions
  1. Study elucidated the structure of the NPr:EIN Ntr complex using a hybrid approach. The structure has a similar fold to the homologous HPr:EIN sugar complex, but differs in surface potential, which explains the difference in specificity between the two evolutionarily related enzyme pairs. PMID: 27839951
  2. Isolated a stable recombinant C-terminal domain of Enzyme I (EIC) of Escherichia coli and characterized its interaction with the N-terminal domain of Enzyme I (EIN) and also with various ligands. PMID: 22936614
  3. Subcellular distribution depends on growth conditions PMID: 15557553
  4. the phosphotransfer rate increases approximately 25-fold when HPr is added to a mixture of EI-N, EI-C, and PEP(Mg(2+)) PMID: 16547354
  5. EI and EI-H189Q each comprise a multiplicity of conformers and progressively fewer conformers as they dimerize and bind Mg(2+) and finally PEP PMID: 16547355
  6. crystal structure reveals a dimeric protein where each subunit comprises three domains PMID: 17053069

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Subcellular Location
Cytoplasm.
Protein Families
PEP-utilizing enzyme family
Database Links
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