P09413 · GVPC_DOLFA

Function

function

Confers stability, involved in shaping gas vesicles (GV), hollow, gas-filled proteinaceous nanostructures. During planktonic growth they allow positioning of the organism at a favorable depth for light or nutrient acquisition (Probable) (Ref.4). The ratio of GvpA:GvpC is estimated to be 25:1 (PubMed:7476201, PubMed:8254305).
GvpC strengthens the GV wall, probably by connecting several GvpA proteins in the same and/or adjacent ribs (Probable) (PubMed:1510555, PubMed:16735729, PubMed:7476201, Ref.5). Removal of GvpC by SDS reduces the critical collapse pressure (CCP) of stored gas vesicles from 0.23 Mpa to 0.08 MPa (Ref.5). Removal of GvpC by urea reduces CCP of freshly isolated GVs from 0.550 MPa to 0.190 MPa; addition of recombinant GvpC restores CCP to 0.508 MPa. As the turgor pressure in this species is usually 0.35 MPa (plus the water column pressure in its growth environment), this protein is essential for GV formation (PubMed:1510555).

Miscellaneous

Protein sequence was derived from constitutive gas vesicle producer strain CCAP 1403/13f, DNA sequence from CCAP 1403/13d, a spontaneous mutant which does not produce gas vesicles.

Biotechnology

Can be used as an oxygen carrier in mammalian cell culture; addition of 1.8% GVs in the medium enhanced the maximum glucose utilization rate by about 30%. The GVs have both GvpA and GvpC.
Engineered gas vesicles (GV) can be used for noninvasive imaging in bacteria and mice. Heterologous GVs with 2 copies of gvpA plus gvpC from this bacteria and the gvpR-gvpU operon from P.megaterium make GVs suitable for imaging of bacteria deep in mouse tissues (e.g. the gastrointestinal tract), or when expressed in tumor-homing bacteria, can be detected in tumors (PubMed:29300010).
Can be used to make acoustic biosensors for ultrasound imaging. Insertion of a protease target site in GvpC and subsequent exposure to the protease leads to GVs that collapse at lower hydrostatic pressures; both endoproteases and processive exoproteases can be used. Controlling GvpC degradation allows controlled GV collapse and changes in ultrasound images (PubMed:32661379).

GO annotations

AspectTerm
Cellular Componentgas vesicle
Biological Processgas vesicle organization

Names & Taxonomy

Protein names

  • Recommended name
    Gas vesicle protein C
  • Short names
    GVPc

Gene names

    • Name
      gvpC

Organism names

Accessions

  • Primary accession
    P09413

Subcellular Location

Gas vesicle
Note: Binds to the entire external surface of the gas vesicle (PubMed:1510555, PubMed:1527496, PubMed:16735729, PubMed:3141741, PubMed:32661379, PubMed:7476201, PubMed:8254305, Ref.5). Trypsin cleaves most of the expected sites in intact vesicles, suggesting all of GvpC is on the surface (PubMed:16735729).

Keywords

Phenotypes & Variants

Features

Showing features for natural variant, mutagenesis.

TypeIDPosition(s)Description
Natural variant3in strain: CCAP 1401/1
Natural variant5-6in strain: CCAP 1401/1
Natural variant16-17in strain: CCAP 1401/1
Mutagenesis85-183Missing last 3 repeats, restores gas vesicle stability 70% as well as wild-type.
Mutagenesis118-183Missing last 2 repeats, restores gas vesicle stability 80% as well as wild-type.
Mutagenesis151-183Missing last repeat, restores gas vesicle stability 80% as well as wild-type.

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 3 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001826631-193Gas vesicle protein C

Expression

Induction

Gas vesicles are abundant in low light, and collapse after exposure to high light.

Structure

Family & Domains

Features

Showing features for repeat, region.

TypeIDPosition(s)Description
Repeat19-51
Region19-1835 X 33 AA tandem repeats
Repeat52-84
Repeat85-117
Repeat118-150
Repeat151-183

Domain

The tandem repeats probably bind across adjacent GvpA ribs with each repeat contacting 5 GvpA subunits, stiffening the vesicle.

Sequence similarities

Belongs to the gas vesicle GvpC family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    193
  • Mass (Da)
    21,986
  • Last updated
    1989-07-01 v1
  • Checksum
    E507CE4BF3927E32
MISLMAKIRQEHQSIAEKVAELSLETREFLSVTTAKRQEQAEKQAQELQAFYKDLQETSQQFLSETAQARIAQAEKQAQELLAFHKELQETSQQFLSATAQARIAQAEKQAQELLAFYQEVRETSQQFLSATAQARIAQAEKQAQELLAFHKELQETSQQFLSATADARTAQAKEQKESLLKFRQDLFVSIFG

Mass Spectrometry

Molecular mass is 21,961 Da. Determined by MALDI.

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
X07544
EMBL· GenBank· DDBJ
CAA30417.1
EMBL· GenBank· DDBJ
Genomic DNA
U17109
EMBL· GenBank· DDBJ
AAA58710.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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