D4GZE7 · SAMP2_HALVD

Function

function

Functions as a protein modifier covalently attached to lysine residues of substrate proteins, as well as a sulfur carrier in tRNA thiolation. The protein modification process is termed sampylation and involves the formation of an isopeptide bond between the SAMP2 C-terminal glycine carboxylate and the epsilon-amino group of lysine residues on target proteins. Is able to form polymeric chains with itself at Lys-58, similar to ubiquitin and other ubiquitin-like proteins. May serve as a proteolytic signal in the cell to target proteins for degradation by proteasomes.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionnucleotide binding
Molecular Functionprotein tag activity
Biological Processprotein modification by small protein conjugation

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Small archaeal modifier protein 2
  • Short names
    SAMP2
  • Alternative names
    • Ubiquitin-like small archaeal modifier protein 2

Gene names

    • Name
      samp2
    • Ordered locus names
      HVO_0202

Organism names

Accessions

  • Primary accession
    D4GZE7

Proteomes

Phenotypes & Variants

Disruption phenotype

Cells lacking this gene grow similarly to wild-type in the presence of either DMSO or oxygen as the terminal electron acceptor, but are retarded in aerobic growth at 50 degrees Celsius. The lysine tRNAs of the mutant strain appear to be nonthiolated.

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis53Abolishes SAMPylation of substrate proteins.
Mutagenesis58Loss of isopeptide linkage of polymeric chains on NcsA; when associated with R-64.
Mutagenesis64Loss of isopeptide linkage of polymeric chains on NcsA; when associated with R-58.
Mutagenesis65-66Abolishes SAMPylation of substrate proteins.

PTM/Processing

Features

Showing features for chain, cross-link, modified residue.

TypeIDPosition(s)Description
ChainPRO_00003971021-66Small archaeal modifier protein 2
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2)
Modified residue661-thioglycine; alternate
Modified residue66Glycyl adenylate; alternate
Cross-link66Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate

Post-translational modification

The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer.

Keywords

Proteomic databases

Interaction

Subunit

Monomer (PubMed:23821306).
Monomeric and polymeric forms interact with NcsA (PubMed:24906001).

Protein-protein interaction databases

Family & Domains

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    66
  • Mass (Da)
    7,118
  • Last updated
    2010-05-18 v1
  • Checksum
    09442B0B845C7DE0
MNVTVEVVGEETSEVAVDDDGTYADLVRAVDLSPHEVTVLVDGRPVPEDQSVEVDRVKVLRLIKGG

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001956
EMBL· GenBank· DDBJ
ADE03392.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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