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Small archaeal modifier protein 3 (SAMP3) (Ubiquitin-like small archaeal modifier protein 3)

 SAMP3_HALVD             Reviewed;          92 AA.
D4GVB0;
14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
14-MAY-2014, sequence version 2.
20-DEC-2017, entry version 37.
RecName: Full=Small archaeal modifier protein 3;
Short=SAMP3;
AltName: Full=Ubiquitin-like small archaeal modifier protein 3;
Name=samp3; OrderedLocusNames=HVO_2177;
Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC
14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
Archaea; Euryarchaeota; Halobacteria; Haloferacales; Haloferacaceae;
Haloferax.
NCBI_TaxID=309800;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
VKM B-1768 / DS2;
PubMed=20333302; DOI=10.1371/journal.pone.0009605;
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.;
"The complete genome sequence of Haloferax volcanii DS2, a model
archaeon.";
PLoS ONE 5:E9605-E9605(2010).
[2]
FUNCTION, AMPYLATION AT GLY-92, AND DISRUPTION PHENOTYPE.
STRAIN=DS2 / DS70;
PubMed=21368171; DOI=10.1073/pnas.1018151108;
Miranda H.V., Nembhard N., Su D., Hepowit N., Krause D.J., Pritz J.R.,
Phillips C., Soll D., Maupin-Furlow J.A.;
"E1- and ubiquitin-like proteins provide a direct link between protein
conjugation and sulfur transfer in archaea.";
Proc. Natl. Acad. Sci. U.S.A. 108:4417-4422(2011).
[3]
FUNCTION AS A PROTEIN MODIFIER, PROTEIN TARGETS, CROSS-LINK,
INDUCTION, MUTAGENESIS OF 91-GLY-GLY-92, AND IDENTIFICATION OF START
SITE.
STRAIN=DS2 / DS70;
PubMed=24097257; DOI=10.1074/mcp.M113.029652;
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.;
"Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a
UbaA-dependent mechanism.";
Mol. Cell. Proteomics 13:220-239(2014).
[4]
STRUCTURE BY NMR, AND SUBUNIT.
STRAIN=DS2;
PubMed=23821306; DOI=10.1002/pro.2305;
Li Y., Maciejewski M.W., Martin J., Jin K., Zhang Y.,
Maupin-Furlow J.A., Hao B.;
"Crystal structure of the ubiquitin-like small archaeal modifier
protein 2 from Haloferax volcanii.";
Protein Sci. 22:1206-1217(2013).
-!- FUNCTION: Functions as a protein modifier covalently attached to
lysine residues of substrate proteins. The protein modification
process is termed sampylation and involves the formation of an
isopeptide bond between the SAMP3 C-terminal glycine carboxylate
and the epsilon-amino group of lysine residues on target proteins.
Seems to be able to form polymeric chains with itself at Lys-18,
Lys-55 and Lys-62, similar to ubiquitin and other ubiquitin-like
proteins. SAMP3 appears not to serve as a proteolytic signal in
the cell to target proteins for degradation by proteasomes. May
regulate molybdenum cofactor (MoCo) biosynthesis by inhibiting the
activity of MPT synthase MoaE under aerobic conditions, providing
a hierarchy of oxygen use prior to that of alternative electron
acceptors such as DMSO. {ECO:0000269|PubMed:21368171,
ECO:0000269|PubMed:24097257}.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23821306}.
-!- INDUCTION: Up-regulated by the addition of dimethyl sulfoxide to
aerobically growing cells. These conditions also increase the
levels of SAMP3 conjugates in cells.
{ECO:0000269|PubMed:24097257}.
-!- PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by
UbaA.
-!- DISRUPTION PHENOTYPE: Cells lacking this gene grow similarly to
wild-type in the presence of either DMSO or oxygen as the terminal
electron acceptor; thus, SAMP3 is not needed for DMSO respiration,
suggesting that it is not required for molybdenum cofactor (MoCo)
biosynthesis. tRNA thiolation is not affected.
{ECO:0000269|PubMed:21368171}.
-!- SEQUENCE CAUTION:
Sequence=ADE02783.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; CP001956; ADE02783.1; ALT_INIT; Genomic_DNA.
RefSeq; WP_004042069.1; NZ_AOHU01000041.1.
PDB; 2M19; NMR; -; A=1-92.
PDBsum; 2M19; -.
SMR; D4GVB0; -.
STRING; 309800.HVO_2177; -.
EnsemblBacteria; ADE02783; ADE02783; HVO_2177.
GeneID; 8923994; -.
KEGG; hvo:HVO_2177; -.
eggNOG; ENOG4102TM3; Archaea.
eggNOG; ENOG410Y0D8; LUCA.
HOGENOM; HOG000280991; -.
KO; K03636; -.
OrthoDB; POG093Z0JVJ; -.
Proteomes; UP000008243; Chromosome.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
Gene3D; 3.10.20.30; -; 1.
InterPro; IPR012675; Beta-grasp_dom_sf.
InterPro; IPR010038; MoaD_arc-typ.
InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
InterPro; IPR003749; ThiS/MoaD-like.
Pfam; PF02597; ThiS; 1.
SUPFAM; SSF54285; SSF54285; 1.
TIGRFAMs; TIGR01687; moaD_arch; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Isopeptide bond; Nucleotide-binding;
Phosphoprotein; Reference proteome; Ubl conjugation;
Ubl conjugation pathway.
CHAIN 1 92 Small archaeal modifier protein 3.
/FTId=PRO_0000428940.
MOD_RES 92 92 Glycyl adenylate; alternate.
{ECO:0000269|PubMed:21368171}.
CROSSLNK 18 18 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SAMP3).
CROSSLNK 55 55 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SAMP3).
CROSSLNK 62 62 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SAMP3).
CROSSLNK 92 92 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins); alternate.
MUTAGEN 91 92 Missing: Abolishes conjugation of SAMP3
to protein targets.
{ECO:0000269|PubMed:24097257}.
STRAND 1 7 {ECO:0000244|PDB:2M19}.
HELIX 10 15 {ECO:0000244|PDB:2M19}.
STRAND 18 25 {ECO:0000244|PDB:2M19}.
HELIX 30 40 {ECO:0000244|PDB:2M19}.
HELIX 42 44 {ECO:0000244|PDB:2M19}.
TURN 45 48 {ECO:0000244|PDB:2M19}.
STRAND 59 62 {ECO:0000244|PDB:2M19}.
STRAND 72 75 {ECO:0000244|PDB:2M19}.
STRAND 82 86 {ECO:0000244|PDB:2M19}.
SEQUENCE 92 AA; 10046 MW; 425F8EA3DE9904A3 CRC64;
MELELRFFAT FREVVGQKSI YWRVDDDATV GDVLRSLEAE YDGLAGRLIE DGEVKPHVNV
LKNGREVVHL DGMATALDDG DAVSVFPPVA GG


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