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/-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

3-7 business days

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.

Description

The recombinant Escherichia coli (strain K12) bamA was expressed with the amino acid range of 175-424. The theoretical molecular weight of the bamA protein is 36.0 kDa. This bamA recombinant protein is manufactured in e.coli. Fusion of the N-terminal 10xHis tag and C-terminal Myc tag into the bamA encoding gene fragment was conducted, allowing for easier detection and purification of the bamA protein in subsequent stages.

Escherichia coli Outer membrane protein assembly factor BamA is a central component of the β-barrel assembly machinery (BAM) complex, crucial for the proper folding and insertion of outer membrane proteins (OMPs). Research on BamA primarily explores its role in outer membrane biogenesis, focusing on understanding its structure, mechanism, and interactions with substrates. Investigations aim to elucidate the intricate processes of protein folding and insertion, providing insights into bacterial outer membrane integrity and potential targets for antimicrobial drug development, crucial for combating bacterial infections and addressing antibiotic resistance.

Target Background

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. 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.

Gene References into Functions

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
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
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
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
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
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
BamD and BamA mutations cause a marked decrease in the levels of multimeric proteins. PMID: 27161117
BamA alone can repeatedly facilitate the folding of OMPs PMID: 26394056
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
structural analysis of BamB bound to a periplasmic domain fragment of BamA, the central component of the beta-barrel assembly machine PMID: 25468906
BamA has five polypeptide transport-associated domains in its N-terminus, all of which are essential for BamA protein function. PMID: 24376817
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
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
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
Pull-down and Western blotting assays indicate that BamB interacts directly with the POTRA 1-3 domain of BamA PMID: 22948914
the conserved (641)RGF(643) residues of the BamA L6 loop are important for BamA folding and biogenesis PMID: 22753067
results imply that BamA and BamD interact directly with outer membrane protein substrates PMID: 22331884
Taken together, these findings suggest that BamE modulates the conformation of BamA, likely through its interactions with BamD. PMID: 22178970
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
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
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
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
the periplasmic chaperone SurA and subunits of the Bam (Omp85) complex catalyse the insertion and assembly of outer-membrane proteins PMID: 19815580
YaeT may have a role in outer membrane protein assembly in E. coli PMID: 15951436
YaeT acts as a general outer membrane proteins assembly factor. PMID: 16102012
YaeT, through its interaction with other outer membrane lipoproteins, forms a functional complex to assemble Escherichia coli membrane protein. PMID: 16824102
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
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
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
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
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
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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Code	CSB-EP364271ENV1
MSDS	MSDS
Size	US$388
	Order now
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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Recombinant Escherichia coli Outer membrane protein assembly factor BamA (BamA), partial

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