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D4GZE7 (SAMP2_HALVD) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Small archaeal modifier protein 2

Short name=SAMP2
Alternative name(s):
Ubiquitin-like small archaeal modifier protein 2
Gene names
Name:samp2
Ordered Locus Names:HVO_0202
OrganismHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii) [Reference proteome] [HAMAP]
Taxonomic identifier309800 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax

Protein attributes

Sequence length66 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.4 Ref.5

Subunit structure

Monomer. Ref.8

Post-translational modification

The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer (Ref.4).

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. Ref.4

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 6666Small archaeal modifier protein 2
PRO_0000397102

Amino acid modifications

Modified residue6611-thioglycine; alternate Probable
Modified residue661Glycyl adenylate; alternate Probable
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2) Ref.2
Cross-link66Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate

Experimental info

Mutagenesis531E → G: Abolishes SAMPylation of substrate proteins. Ref.2 Ref.8
Mutagenesis65 – 662Missing: Abolishes SAMPylation of substrate proteins. Ref.2

Secondary structure

................. 66
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
D4GZE7 [UniParc].

Last modified May 18, 2010. Version 1.
Checksum: 09442B0B845C7DE0

FASTA667,118
        10         20         30         40         50         60 
MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ SVEVDRVKVL 


RLIKGG 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome sequence of Haloferax volcanii DS2, a model archaeon."
Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.
PLoS ONE 5:E9605-E9605(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[2]"Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax volcanii."
Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G., Chen S., Wells L., Maupin-Furlow J.A.
Nature 463:54-60(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS A PROTEIN MODIFIER, CROSS-LINK, PROTEIN TARGETS, SAMPYLATION AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF 65-GLY-GLY-66.
Strain: ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2.
[3]"SAMPyling proteins in archaea."
Darwin K.H., Hofmann K.
Trends Biochem. Sci. 35:348-351(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[4]"E1- and ubiquitin-like proteins provide a direct link between protein conjugation and sulfur transfer in archaea."
Miranda H.V., Nembhard N., Su D., Hepowit N., Krause D.J., Pritz J.R., Phillips C., Soll D., Maupin-Furlow J.A.
Proc. Natl. Acad. Sci. U.S.A. 108:4417-4422(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE.
Strain: DS2 / DS70.
[5]"Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-dependent mechanism."
Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J., Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L., Maupin-Furlow J.A.
Mol. Cell. Proteomics 13:220-239(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
Strain: DS2 / DS70.
[6]"Solution structure of ubiquitin-like small archaeal modifier protein in Haloferax volcanii."
Fan S., Zhang W., Liao S., Tu X.
Submitted (SEP-2010) to the PDB data bank
Cited for: STRUCTURE BY NMR.
[7]"Structure of a protein from Haloferax volcanii."
Liao S., Zhang W., Fan K., Tu X.
Submitted (SEP-2011) to the PDB data bank
Cited for: STRUCTURE BY NMR.
[8]"Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii."
Li Y., Maciejewski M.W., Martin J., Jin K., Zhang Y., Maupin-Furlow J.A., Hao B.
Protein Sci. 22:1206-1217(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, MUTAGENESIS OF GLU-53.
Strain: DS2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001956 Genomic DNA. Translation: ADE03392.1.
RefSeqYP_003534279.1. NC_013967.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2L32NMR-A1-66[»]
2LJINMR-A1-66[»]
4HRSX-ray2.30A2-66[»]
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADE03392; ADE03392; HVO_0202.
GeneID8926718.
KEGGhvo:HVO_0202.

Phylogenomic databases

HOGENOMHOG000227894.
KOK03154.
OMAPEDQPVE.

Enzyme and pathway databases

BioCycHVOL309800:GCOK-206-MONOMER.

Family and domain databases

Gene3D3.10.20.30. 1 hit.
InterProIPR012675. Beta-grasp_dom.
IPR016155. Mopterin_synth/thiamin_S_b.
[Graphical view]
SUPFAMSSF54285. SSF54285. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceD4GZE7.

Entry information

Entry nameSAMP2_HALVD
AccessionPrimary (citable) accession number: D4GZE7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references