Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of a mutant strain HM1052, a DELTAubaA E1-like mutant | Haloferax volcanii |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Haloferax volcanii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii YW1001 | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | Haloferax volcanii | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | Haloferax volcanii YW1001 | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | - |
AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii | - |
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii YW1001 | - |
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | - |
AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
additional information | Haloferax volcanii | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | ? | - |
? | |
additional information | Haloferax volcanii YW1001 | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | ? | - |
? | |
additional information | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Haloferax volcanii | D4GSF3 | - |
- |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | D4GSF3 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
additional information | many of the sampylated proteins that are identified are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | Haloferax volcanii |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii YW1001 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | - |
Haloferax volcanii | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | - |
Haloferax volcanii YW1001 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP1]-Gly-Gly + [UbaA]-L-cysteine | - |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | AMP + diphosphate + N6-[[SAMP1]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii YW1001 | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [protein]-L-lysine | - |
Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[protein]-L-lysine] | - |
? | |
ATP + [SAMP3]-Gly-Gly + [UbaA]-L-cysteine | - |
Haloferax volcanii | AMP + diphosphate + N6-[[SAMP3]-Gly-Gly]-[[UbaA]-L-cysteine] | - |
? | |
additional information | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | Haloferax volcanii | ? | - |
? | |
additional information | the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif | Haloferax volcanii | ? | - |
? | |
additional information | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | Haloferax volcanii YW1001 | ? | - |
? | |
additional information | the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif | Haloferax volcanii YW1001 | ? | - |
? | |
additional information | many of the sampylated proteins that are identified (from cells grown aerobically on DMSO) are homologues of sulfur metabolism, oxidative stress, and/or autoregulation. Proteins found multiply modified by sampylation are examples of this association including the E1-like UbaA, the ubiquitin-like SAMP3 (related to SAMP1), the large subunit of MPT synthase (MoaE), and a methionine sulfoxide-S-reductase homologue (MsrA) | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | ? | - |
? | |
additional information | the SAMP1 S85R variant is found functional in sulfur mobilization and isopeptide linkage. Addition of DMSO to the culture medium increased the diversity of SAMP1 S85R conjugates in a banding pattern that is comparable to wild-type but distinct from SAMP1 S85K. Of the SAMPs encoded on the genome of Haloferax volcanii, only SAMP2 has a native (R/K) preceding the C-terminal di-Gly motif | Haloferax volcanii ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
E1-like UbaA | - |
Haloferax volcanii |
SAMP-activating E1 enzyme | - |
Haloferax volcanii |
UbaA | - |
Haloferax volcanii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Haloferax volcanii |
General Information | Comment | Organism |
---|---|---|
additional information | the crystal structure of SAMP1, PDB ID 3PO0, is docked to the three-dimensional model of UbaA using the Escherichia coli MoaD-MoeB complex as a template, PDB ID 1JW9. Enzyme UbaA dimeric complex structure modeling, and ab initio modeling of the remaining 25 residues of UbaA, which include the highly disordered N- and C-termini | Haloferax volcanii |
physiological function | the archaeon Haloferax volcanii uses SAMP1 as a protein modifier to regulate and orchestrate cellular functions. SAMP1 is ligated to proteins by transfer via SAMP-activating E1 enzyme UbaA, i.e. samp1ylation. SAMP1 is a ubiquitin-like protein modifier that is relatively specific in tagging its protein partners as well as proteins associated with oxidative stress response. SAMP1 modifies a relatively small number of protein targets. SAMPs are activated (adenylated) in an ATP-dependent manner by the E1-like UbaA/ELSA and liberated from SAMP conjugates by the action of the JAMM/MPN+ Zn2+-metalloprotease HvJAMM1. SAMP1 conjugation is speculated to regulate the catalytic activity of MPT synthase, the conserved K240 and K247 residues of MoaE, the large subunit of MPT synthase, are found to be covalently attached to C-terminus of SAMP1 | Haloferax volcanii |