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D4GZE7

- SAMP2_HALVD

UniProt

D4GZE7 - SAMP2_HALVD

Protein

Small archaeal modifier protein 2

Gene

samp2

Organism
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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.3 Publications

    GO - Molecular functioni

    1. nucleotide binding Source: UniProtKB-KW
    2. protein tag Source: UniProtKB

    GO - Biological processi

    1. protein modification by small protein conjugation Source: UniProtKB

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Nucleotide-binding

    Enzyme and pathway databases

    BioCyciHVOL309800:GCOK-206-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Small archaeal modifier protein 2
    Short name:
    SAMP2
    Alternative name(s):
    Ubiquitin-like small archaeal modifier protein 2
    Gene namesi
    Name:samp2
    Ordered Locus Names:HVO_0202
    OrganismiHaloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
    Taxonomic identifieri309800 [NCBI]
    Taxonomic lineageiArchaeaEuryarchaeotaHalobacteriaHalobacterialesHalobacteriaceaeHaloferax
    ProteomesiUP000008243: Chromosome

    Pathology & Biotechi

    Disruption phenotypei

    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.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi53 – 531E → G: Abolishes SAMPylation of substrate proteins. 2 Publications
    Mutagenesisi65 – 662Missing: Abolishes SAMPylation of substrate proteins. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 6666Small archaeal modifier protein 2PRO_0000397102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki58 – 58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2)
    Modified residuei66 – 6611-thioglycine; alternateCurated
    Modified residuei66 – 661Glycyl adenylate; alternateCurated
    Cross-linki66 – 66Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins); alternate

    Post-translational modificationi

    The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA, and also probably thiocarboxylated (-COSH) to function in sulfur transfer.1 Publication

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    Secondary structure

    1
    66
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 65
    Beta strandi12 – 165
    Helixi23 – 297
    Helixi34 – 363
    Beta strandi39 – 413
    Beta strandi44 – 463
    Helixi47 – 493
    Beta strandi50 – 534
    Beta strandi57 – 593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2L32NMR-A1-66[»]
    2LJINMR-A1-66[»]
    4HRSX-ray2.30A2-66[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiD4GZE7.

    Family & Domainsi

    Phylogenomic databases

    HOGENOMiHOG000227894.
    KOiK03154.
    OMAiPEDQPVE.

    Family and domain databases

    Gene3Di3.10.20.30. 1 hit.
    InterProiIPR012675. Beta-grasp_dom.
    IPR016155. Mopterin_synth/thiamin_S_b.
    [Graphical view]
    SUPFAMiSSF54285. SSF54285. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    D4GZE7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ   50
    SVEVDRVKVL RLIKGG 66
    Length:66
    Mass (Da):7,118
    Last modified:May 18, 2010 - v1
    Checksum:i09442B0B845C7DE0
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001956 Genomic DNA. Translation: ADE03392.1.
    RefSeqiYP_003534279.1. NC_013967.1.

    Genome annotation databases

    EnsemblBacteriaiADE03392; ADE03392; HVO_0202.
    GeneIDi8926718.
    KEGGihvo:HVO_0202.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CP001956 Genomic DNA. Translation: ADE03392.1 .
    RefSeqi YP_003534279.1. NC_013967.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2L32 NMR - A 1-66 [» ]
    2LJI NMR - A 1-66 [» ]
    4HRS X-ray 2.30 A 2-66 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai ADE03392 ; ADE03392 ; HVO_0202 .
    GeneIDi 8926718.
    KEGGi hvo:HVO_0202.

    Phylogenomic databases

    HOGENOMi HOG000227894.
    KOi K03154.
    OMAi PEDQPVE.

    Enzyme and pathway databases

    BioCyci HVOL309800:GCOK-206-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei D4GZE7.

    Family and domain databases

    Gene3Di 3.10.20.30. 1 hit.
    InterProi IPR012675. Beta-grasp_dom.
    IPR016155. Mopterin_synth/thiamin_S_b.
    [Graphical view ]
    SUPFAMi SSF54285. SSF54285. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. 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. 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. 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.

    Entry informationi

    Entry nameiSAMP2_HALVD
    AccessioniPrimary (citable) accession number: D4GZE7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 10, 2010
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 29 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references

    External Data

    Dasty 3