Recombinant Escherichia coli Outer membrane protein assembly factor BamA(BamA),partial

Code CSB-EP364271ENV1
Size US$2466
Image
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP364271ENV1 could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) bamA.
  • Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of CSB-EP364271ENV1 could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) bamA.
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Product Details

Purity Greater than 90% as determined by SDS-PAGE.
Target Names bamA
Uniprot No. P0A940
Research Area Others
Alternative Names bamA; yaeT; yzzN; yzzY; b0177; JW0172Outer membrane protein assembly factor BamA; Omp85
Species Escherichia coli (strain K12)
Source E.coli
Expression Region 175-424aa
Target Protein Sequence AEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTG
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight 36.0 kDa
Protein Length Partial
Tag Info N-terminal 10xHis-tagged and C-terminal Myc-tagged
Form Liquid or 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 Tris-based buffer,50% glycerol
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°C/-80°C. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting
and FAQs
Protein FAQs
Storage Condition Store at -20°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 Basically, we can dispatch the products out in 1-3 working days after receiving your orders. 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 & COA Please contact us to get it.

Target Data

Function Part of the outer membrane protein assembly complex (Bam), which is involved in assembly and insertion of beta-barrel proteins into the outer membrane. Constitutes, with BamD, the core component of the assembly machinery. Efficient substrate folding and insertion into the outer membrane requires all 5 subunits
Gene References into Functions
  1. Free-energy calculations of lateral gate opening revealed a significantly lower barrier to opening in the C-terminal kinked conformation; mutagenesis experiments confirm the relevance of C-terminal kinking to BamA structure and function. PMID: 30087180
  2. Studied how the Bam complex accelerates folding and insertion through the assembly of a slow-folding beta-barrel substrate, LptD. Results suggest a mechanism in which substrate recruitment by periplasmic BamD regulates extracellular loop interactions to activate BamA for folding and insertion. PMID: 29463713
  3. we studied the assembly of an essential beta-barrel substrate for the Bam complex, BamA. By mutating conserved residues in the beta-barrel domain of this protein, we generated three assembly-defective BamA substrates that stall early in the folding process in the periplasm. Two of the three defective substrates, which harbor mutations within beta-strands, fail to associate productively with the Bam complex PMID: 28223520
  4. Data show that LptD is folded around LptE, and both components interact with the two essential beta-barrel assembly machine (Bam) components, BamA and BamD. PMID: 27439868
  5. The authors show that electrostatic interactions between the two essential proteins BamA and BamD coordinate conformational changes upon binding of unfolded substrate that allow the assembly reaction to proceed. PMID: 28760846
  6. Study investigated BamA flexibility using molecular dynamics simulations of BamA embedded in a model Escherichia coli outer membrane, reported that POTRA-membrane interactions influence the set of observed conformations PMID: 27332128
  7. BamD and BamA mutations cause a marked decrease in the levels of multimeric proteins. PMID: 27161117
  8. BamA alone can repeatedly facilitate the folding of OMPs PMID: 26394056
  9. Data show that disulfide crosslinks prevented lateral opening and exit pore formation resulting in a loss of outer membrane proteins BamA function, which can be fully rescued by the reductant tris(2-carboxyethyl)phosphine. PMID: 24980798
  10. structural analysis of BamB bound to a periplasmic domain fragment of BamA, the central component of the beta-barrel assembly machine PMID: 25468906
  11. BamA has five polypeptide transport-associated domains in its N-terminus, all of which are essential for BamA protein function. PMID: 24376817
  12. study determined the crystal structure of the C-terminal transmembrane domain of BamA at 2.6 A resolution; findings suggest the dome over the barrel may play an important role in maintaining the efficiency of OMP biogenesis PMID: 24619089
  13. These results suggest that the periplasmic region of BamA is firmly attached to the beta-barrel and does not experience fast global motion around the angle between POTRA 2 and 3. PMID: 24530687
  14. Our direct coupling analysis of BamA implicates residues R661 and D740 in a functional interaction. We find that the substitutions R661G and D740G each confer OM permeability defects and destabilize the BamA b-barrel PMID: 23934888
  15. Pull-down and Western blotting assays indicate that BamB interacts directly with the POTRA 1-3 domain of BamA PMID: 22948914
  16. the conserved (641)RGF(643) residues of the BamA L6 loop are important for BamA folding and biogenesis PMID: 22753067
  17. results imply that BamA and BamD interact directly with outer membrane protein substrates PMID: 22331884
  18. Taken together, these findings suggest that BamE modulates the conformation of BamA, likely through its interactions with BamD. PMID: 22178970
  19. Conditions that increase the folding of BamA demonstrate the ability of the reconstituted complex to catalyze more than one round of substrate assembly. PMID: 21823654
  20. the crystal structure of BamA POTRA4-5 has been determined to 1.50 A resolution with an R factor of 14.7% and an Rfree of 18.9% PMID: 21795783
  21. The data suggest that SurA and BamA POTRA 1 domain function in concert to assist folding and assembly of most beta-barrel outer membrane proteins except for TolC. PMID: 20598079
  22. The authors demonstrate that (i) BamA is essential for biogenesis of the trimeric auotransporter adhesins YadA, (ii) BamA interacts directly with YadA, (iii) the C-terminal amino acid motif of YadA is important for the BamA-dependent assembly. PMID: 20815824
  23. the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex catalyse the insertion and assembly of outer-membrane proteins PMID: 19815580
  24. YaeT may have a role in outer membrane protein assembly in E. coli PMID: 15951436
  25. YaeT acts as a general outer membrane proteins assembly factor. PMID: 16102012
  26. YaeT, through its interaction with other outer membrane lipoproteins, forms a functional complex to assemble Escherichia coli membrane protein. PMID: 16824102
  27. YaeT is composed of two distinct domains, an amino-terminal periplasmic and a carboxy-terminal membrane domain; the periplasmic domain proves to be essential for in vivo function of YaeT PMID: 16829683
  28. Here we show that an essential and highly conserved gene product, YaeT, is the surface molecule recognized by the majority (ca. 70%) of Stx phages via conserved tail spike proteins PMID: 17693515
  29. crystal structure of a periplasmic fragment of YaeT reveals the polypeptide transport-associated (POTRA) domain fold and suggests a model for how POTRA domains can bind different peptide sequences PMID: 17702946
  30. Data show that YaeT-YfgL interaction invloves the region encompassing L173, L175, and R176 of YfgL and it was found that altering residues D227 and D229 in another region of YfgL from E221 to D229 resulted in defective YaeT bindings. PMID: 18165306
  31. Characterization of mutants resistant to contact-dependent growth inhibition (CDI) allowed the authors to identify BamA (YaeT) as the outer membrane receptor for CDI and AcrB as a potential downstream target. PMID: 18761695
  32. 1H, 13C and 15N chemical shift assignments and secondary structure of the YaeT POTRA domain; a domain found in the Omp85 family of proteins which is critical for insertion and folding of outer membrane proteins in Gram-negative bacteria PMID: 19636842

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Subcellular Location Cell outer membrane
Protein Families BamA family
Database Links

KEGG: ecj:JW0172

STRING: 316385.ECDH10B_0157

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