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

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中文名稱：

Recombinant Escherichia coli Outer membrane protein assembly factor BamA(BamA),partial
品名簡稱：

Recombinant E.coli bamA protein, partial
貨號：

CSB-EP364271ENV1
說明書：

MSDS Datasheet
規(guī)格：

￥2328
圖片：
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.
其他：

產(chǎn)品詳情
產(chǎn)品評價
相關(guān)產(chǎn)品
靶點詳情

產(chǎn)品詳情

純度：

Greater than 90% as determined by SDS-PAGE.
基因名：

bamA
Uniprot No.：

P0A940
別名：

bamA; yaeT; yzzN; yzzY; b0177; JW0172Outer membrane protein assembly factor BamA; Omp85
種屬：

Escherichia coli (strain K12)
蛋白長度：

Partial
來源：

E.coli
分子量：

36.0 kDa
表達區(qū)域：

175-424aa
氨基酸序列

AEIQQINIVGNHAFTTDELISHFQLRDEVPWWNVVGDRKYQKQKLAGDLETLRSYYLDRGYARFNIDSTQVSLTPDKKGIYVTVNITEGDQYKLSGVEVSGNLAGHSAEIEQLTKIEPGELYNGTKVTKMEDDIKKLLGRYGYAYPRVQSMPEINDADKTVKLRVNVDAGNRFYVRKIRFEGNDTSKDAVLRREMRQMEGAWLGSDLVDQGKERLNRLGFFETVDTDTQRVPGSPDQVDVVYKVKERNTG
Note: The complete sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application, please explicitly request the full and complete sequence of this protein before ordering.
蛋白標簽：

N-terminal 10xHis-tagged and C-terminal Myc-tagged
產(chǎn)品提供形式：

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.
緩沖液：

If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.
Note: If you have any special requirement for the glycerol content, please remark when you place the order.
If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose.
儲存條件：

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
保質(zhì)期：

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.
貨期：

3-7 business days
注意事項：

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.

產(chǎn)品評價

靶點詳情

功能：

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. A lateral gate may open between the first and last strands of the BamA beta-barrel that allows substrate to insert into the outer membrane; comparison of the structures of complete and nearly complete Bam complexes show there is considerable movement of all 5 proteins.; (Microbial infection) Acts as a receptor for CdiA-EC93, the contact-dependent growth inhibition (CDI) effector of E.coli strain EC93; antibodies against extracellular epitopes decrease CDI. Its role in CDI is independent of the other Bam complex components. Is not the receptor for CdiA from E.coli strain 536 / UPEC, which does not have the same mode of toxicity as CdiA from strain EC93; the decreased expression of bamA101 in some experiments decreases the level of outer membrane proteins in general. Susceptibility to CdiA-EC93 is dependent on E.coli BamA; replacing BamA with the gene from S.typhimurium LT2, E.cloacae ATCC 13047 or D.dadantii 3937 renders cells resistant to CdiA-EC93. Cells with BamA from another bacteria no longer form CdiA-EC93-induced aggregates with EC93 cells. A chimera in which E.cloacae extracellular loops 6 and 7 are replaced with loops 6 and 7 from E.coli is susceptible to CdiA-EC93 and to CdiA-CT from strain 536 / UPEC.
基因功能參考文獻：
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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亞細胞定位：

Cell outer membrane.
蛋白家族：

BamA family
數(shù)據(jù)庫鏈接：

KEGG: ecj:JW0172

STRING: 316385.ECDH10B_0157