B1VB63 · PDUB_CITFR
- ProteinBacterial microcompartment shell protein PduB
- GenepduB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids270 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
The two proteins produced are among the major shell proteins of the bacterial microcompartment (BMC) shell dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression of the gene gives large amorphous intracellular structures; when only PduB is overexpressed large circular bodies are observed which contain concentric rings, whereas with PduB' overexpression internal bodies with regular straight-lined structures were generated (PubMed:18332146).
The N-terminus of the long form (PduB) is required for correct formation of BMCs. May play a major role in binding the enzyme contents to the shell (By similarity).
The N-terminus of the long form (PduB) is required for correct formation of BMCs. May play a major role in binding the enzyme contents to the shell (By similarity).
Expression of a cosmid containing the full 21-gene pdu operon in E.coli allows E.coli to grow on 1,2-propanediol (1,2-PD) with the appearance of BMCs in its cytoplasm.
The 1,2-PD-specific bacterial microcompartment (BMC) concentrates low levels of 1,2-PD catabolic enzymes, concentrates volatile reaction intermediates thus enhancing pathway flux and keeps the level of toxic, mutagenic propionaldehyde low.
Biotechnology
Artificial BMCs can be made in E.coli by expressing pduA-pduB/B'-pduJ-pduK-pduN-pduU-pduT (in this order); pduT and pduU are optional, while pduA, pduB/B', pduJ, pduK and pduN are essential. A construct with the reversed gene order does not make BMCs (PubMed:20417607).
Ethanogenic BMCs can be made in E.coli by targeting pyruvate decarboxylase (pdc) and alcohol dehydrogenase (adh) to them. PduP(1-18)-Pdc and PduD(1-18)-Adh strains targeted to the BMC (PduA, PduB, PduJ, PduK, PduN, PduU) make significantly more ethanol than strains where Pdc and Adh are not targeted to the BMC (PubMed:24933391).
Ethanogenic BMCs can be made in E.coli by targeting pyruvate decarboxylase (pdc) and alcohol dehydrogenase (adh) to them. PduP(1-18)-Pdc and PduD(1-18)-Adh strains targeted to the BMC (PduA, PduB, PduJ, PduK, PduN, PduU) make significantly more ethanol than strains where Pdc and Adh are not targeted to the BMC (PubMed:24933391).
Pathway
Polyol metabolism; 1,2-propanediol degradation.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | bacterial microcompartment | |
Molecular Function | structural molecule activity | |
Biological Process | propanediol catabolic process |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameBacterial microcompartment shell protein PduB
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Citrobacter > Citrobacter freundii complex
Accessions
- Primary accessionB1VB63
Subcellular Location
Phenotypes & Variants
Disruption phenotype
When the whole pdu operon except this gene is expressed in E.coli no BMCs are made; with the whole operon many BMCs are produced in E.coli.
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 38 | PduB' no longer produced in E.coli. | ||||
Sequence: M → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000454247 | 1-270 | Bacterial microcompartment shell protein PduB | |||
Sequence: MSSNELVDQIMAQVIARVATPEQQAIPENNPPTRETAMAEKSCSLTEFVGTAIGDTVGLVIANVDSALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTFGDVYANEAGHIEMQYTARASYALEKAFGAPIGRACGVIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVISAREIGKTVLGTLGSEPKNDRPSYI |
Post-translational modification
In purified BMCs seen as a 30.0 kDa and 25.0 kDa form; the smaller form is called PduB'.
Interaction
Subunit
Homotrimerizes to form a pseudohexamer with a central pore. The trimers pack into an array (By similarity).
Both forms interact with shell protein PduA (PubMed:20417607).
Both forms interact with shell protein PduA (PubMed:20417607).
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 47-152 | BMC circularly permuted 1 | ||||
Sequence: EFVGTAIGDTVGLVIANVDSALLDAMKLEKRYRSIGILGARTGAGPHIMAADEAVKATNTEVVSIELPRDTKGGAGHGSLIILGGNDVSDVKRGIEVALKELDRTF | ||||||
Domain | 154-262 | BMC circularly permuted 2 | ||||
Sequence: DVYANEAGHIEMQYTARASYALEKAFGAPIGRACGVIVGAPASVGVLMADTALKSANVEVVAYSSPAHGTSFSNEAILVISGDSGAVRQAVISAREIGKTVLGTLGSEP |
Domain
Has 2 BMC domains which can evolve independently of each other.
Sequence similarities
Belongs to the EutL/PduB family.
Family and domain databases
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative promoter usage.
B1VB63-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- NamePduB
- Length270
- Mass (Da)28,022
- Last updated2008-05-20 v1
- Checksum8B0A46B03E5943F1
B1VB63-2
- NamePduB'
- Differences from canonical
- 1-37: Missing
Features
Showing features for alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_061271 | 1-37 | in isoform PduB' | |||
Sequence: Missing |
Keywords
- Coding sequence diversity