D0KZ73 · CSOSD_HALNC

Function

function

Part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, cbbL-cbbS) is sequestered. It may control transport of RuBisCO reactants in and out of the carboxysome (By similarity).
In an E.coli expression system not absolutely necessary, its presence leads to fewer defective carboxysomes, suggesting this subunit may play a role in assembly (PubMed:22184212).
Unlike beta-carboxysomes, alpha-carboxysomes (Cb) can form without cargo protein. CsoS2 is essential for Cb formation and is also capable of targeting foreign proteins to the Cb. The Cb shell assembles with the aid of CsoS2; CsoS1A, CsoS1B and CsoS1C form the majority of the shell while CsoS4A and CsoS4B form vertices. CsoS1D forms pseudohexamers that probably control metabolite flux into and out of the shell.

Biotechnology

Expression of 10 genes for alpha-carboxysome (Cb) proteins (cbbL-cbbS-csoS2-csoS3-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-csoS1D) in E.coli generates compartments that resemble Cb, contain RuBisCO and have its catalytic activity, showing it is possible to make artificial, functional Cb using these 10 genes. Cargo proteins can be targeted to these organelles (PubMed:22184212).
Artificial Cb assembly in E.coli requires csoS2-csoS4A-csoS4B-csoS1C-csoS1A-csoS1B-csoS1D (but not the gene for carbonic anhydrase, csoS3). Targeting proteins to the organelle requires at least one of the CsoS2 C-repeats; 3 repeats gives the best localization. A nanoreactor of the Cb shell proteins has been engineered which generates H2 using a ferredoxin-hydrogenase fusion (AC P07839-Q9FYU1) and a flavodoxin/ferredoxin--NADP reductase (AC A0A0K3QZA5) targeted separately to the Cb; the hydrogenase has first to be matured and activated by HydGXEF (AC Q8EAH9, Q8EAH8, Q8EAH7 and Q8EAH6 respectively). Encapsulation increases H2 production about 20% during anaerobic growth, and over 4-fold more during aerobic growth (PubMed:33116131).

GO annotations

AspectTerm
Cellular Componentcarboxysome
Biological Processcarbon fixation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Carboxysome shell protein CsoS1D

Gene names

    • Name
      csoS1D
    • Ordered locus names
      Hneap_0903

Organism names

Accessions

  • Primary accession
    D0KZ73

Proteomes

Subcellular Location

Carboxysome
Note: This bacterium makes alpha-type carboxysomes.

Keywords

Phenotypes & Variants

Disruption phenotype

Not required for growth in ambient air.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004520751-213Carboxysome shell protein CsoS1D

Interaction

Subunit

Homotrimer. Forms a dimer of stacked trimers, the same faces interact. Probably forms a CsoS1-CsoS1D-CsoS2 complex.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, motif.

TypeIDPosition(s)Description
Domain5-106BMC circularly permuted 1
Motif70-71Gates the pore
Domain108-213BMC circularly permuted 2

Domain

Contains 2 BMC domains, trimerizes in a staggered manner to give a hexamer; each subunit in one trimer interacts with 2 subunits in the facing trimer. Each stacked hexamer can form a pore of about 14 Angstroms in diameter. Dimerization of the trimers forms a channel-like compartment, accessible via an open pore. This channel may be large enough to accomodate transport of substrates into and out of the carboxysome.

Sequence similarities

Belongs to the EutL/PduB family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    213
  • Mass (Da)
    23,451
  • Last updated
    2009-12-15 v1
  • Checksum
    12BD98417A6A61E9
MNNIDLRVYSFIDSLQPQLASYLATSSQGFLPVPGDACLWIEVAPGMAVHRLSDIALKATNVRLGEQVVERAFGSMEIHYRNQSDVLASGEAVLREINHAQEDRLPCRIAWKEIIRAITPDHATLINRQLRKGSMLLPGKSMFILETEPAGYIVQAANEAEKAAHVTLIDVRAFGNFGRLTMMGSEAETEEAMRAAEATIASINARARRAEGF

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001801
EMBL· GenBank· DDBJ
ACX95746.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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