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D4GZE7

- SAMP2_HALVD

UniProt

D4GZE7 - SAMP2_HALVD

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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

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
Complete GO annotation...

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. 1 Publication
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 – 65Combined sources
Beta strandi12 – 165Combined sources
Helixi23 – 297Combined sources
Helixi34 – 363Combined sources
Beta strandi39 – 413Combined sources
Beta strandi44 – 463Combined sources
Helixi47 – 493Combined sources
Beta strandi50 – 534Combined sources
Beta strandi57 – 593Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ
60
SVEVDRVKVL RLIKGG
Length:66
Mass (Da):7,118
Last modified:May 18, 2010 - v1
Checksum:i09442B0B845C7DE0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001956 Genomic DNA. Translation: ADE03392.1.
RefSeqiWP_004045316.1. NZ_AOHU01000106.1.
YP_003534279.1. NC_013967.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001956 Genomic DNA. Translation: ADE03392.1 .
RefSeqi WP_004045316.1. NZ_AOHU01000106.1.
YP_003534279.1. NC_013967.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 31 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