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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: 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

  • nucleotide binding Source: UniProtKB-KW
  • protein tag Source: UniProtKB

GO - Biological processi

  • protein modification by small protein conjugation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Nucleotide-binding

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 lineageiArchaeaEuryarchaeotaHalobacteriaHaloferacalesHaloferacaceaeHaloferax
Proteomesi
  • UP000008243 Componenti: 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)DescriptionActionsGraphical viewLength
Mutagenesisi53E → G: Abolishes SAMPylation of substrate proteins. 1 Publication1
Mutagenesisi65 – 66Missing : Abolishes SAMPylation of substrate proteins. 1 Publication2

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003971021 – 66Small archaeal modifier protein 2Add BLAST66

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SAMP2)
Modified residuei661-thioglycine; alternateCurated1
Modified residuei66Glycyl adenylate; alternateCurated1
Cross-linki66Glycyl 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

Protein-protein interaction databases

STRINGi309800.HVO_0202.

Structurei

Secondary structure

166
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi2 – 6Combined sources5
Beta strandi12 – 16Combined sources5
Helixi23 – 29Combined sources7
Helixi34 – 36Combined sources3
Beta strandi39 – 41Combined sources3
Beta strandi44 – 46Combined sources3
Helixi47 – 49Combined sources3
Beta strandi50 – 53Combined sources4
Beta strandi57 – 59Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L32NMR-A1-66[»]
2LJINMR-A1-66[»]
4HRSX-ray2.30A2-66[»]
SMRiD4GZE7.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiD4GZE7.

Family & Domainsi

Phylogenomic databases

eggNOGiarCOG00535. Archaea.
COG2104. LUCA.
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.

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.
RefSeqiWP_004045316.1. NZ_AOHU01000106.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2L32NMR-A1-66[»]
2LJINMR-A1-66[»]
4HRSX-ray2.30A2-66[»]
SMRiD4GZE7.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi309800.HVO_0202.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiarCOG00535. Archaea.
COG2104. LUCA.
HOGENOMiHOG000227894.
KOiK03154.
OMAiPEDQPVE.

Miscellaneous databases

EvolutionaryTraceiD4GZE7.

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.
ProtoNetiSearch...

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 2, 2016
This is version 39 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.