SAMP2_HALVD
ID SAMP2_HALVD Reviewed; 66 AA.
AC D4GZE7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Small archaeal modifier protein 2;
DE Short=SAMP2;
DE AltName: Full=Ubiquitin-like small archaeal modifier protein 2;
GN Name=samp2; OrderedLocusNames=HVO_0202;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP FUNCTION AS A PROTEIN MODIFIER, CROSS-LINK, PROTEIN TARGETS, SAMPYLATION AT
RP LYS-58, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
RP 65-GLY-GLY-66.
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20054389; DOI=10.1038/nature08659;
RA Humbard M.A., Miranda H.V., Lim J.M., Krause D.J., Pritz J.R., Zhou G.,
RA Chen S., Wells L., Maupin-Furlow J.A.;
RT "Ubiquitin-like small archaeal modifier proteins (SAMPs) in Haloferax
RT volcanii.";
RL Nature 463:54-60(2010).
RN [3]
RP REVIEW.
RX PubMed=20547064; DOI=10.1016/j.tibs.2010.03.003;
RA Darwin K.H., Hofmann K.;
RT "SAMPyling proteins in archaea.";
RL Trends Biochem. Sci. 35:348-351(2010).
RN [4]
RP FUNCTION, THIOCARBOXYLATION AT GLY-66, AMPYLATION AT GLY-66, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=DS2 / DS70;
RX PubMed=21368171; DOI=10.1073/pnas.1018151108;
RA Miranda H.V., Nembhard N., Su D., Hepowit N., Krause D.J., Pritz J.R.,
RA Phillips C., Soll D., Maupin-Furlow J.A.;
RT "E1- and ubiquitin-like proteins provide a direct link between protein
RT conjugation and sulfur transfer in archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:4417-4422(2011).
RN [5]
RP FUNCTION.
RC STRAIN=DS2 / DS70;
RX PubMed=24097257; DOI=10.1074/mcp.m113.029652;
RA Miranda H.V., Antelmann H., Hepowit N., Chavarria N.E., Krause D.J.,
RA Pritz J.R., Basell K., Becher D., Humbard M.A., Brocchieri L.,
RA Maupin-Furlow J.A.;
RT "Archaeal ubiquitin-like SAMP3 is isopeptide-linked to proteins via a UbaA-
RT dependent mechanism.";
RL Mol. Cell. Proteomics 13:220-239(2014).
RN [6]
RP INTERACTION WITH NCSA, AND MUTAGENESIS OF LYS-58 AND LYS-64.
RC STRAIN=DS2 / DS70 {ECO:0000303|PubMed:24906001};
RX PubMed=24906001; DOI=10.1371/journal.pone.0099104;
RA Chavarria N.E., Hwang S., Cao S., Fu X., Holman M., Elbanna D.,
RA Rodriguez S., Arrington D., Englert M., Uthandi S., Soell D.,
RA Maupin-Furlow J.A.;
RT "Archaeal Tuc1/Ncs6 homolog required for wobble uridine tRNA thiolation is
RT associated with ubiquitin-proteasome, translation, and RNA processing
RT system homologs.";
RL PLoS ONE 9:e99104-e99104(2014).
RN [7]
RP STRUCTURE BY NMR.
RA Fan S., Zhang W., Liao S., Tu X.;
RT "Solution structure of ubiquitin-like small archaeal modifier protein in
RT Haloferax volcanii.";
RL Submitted (SEP-2010) to the PDB data bank.
RN [8]
RP STRUCTURE BY NMR.
RA Liao S., Zhang W., Fan K., Tu X.;
RT "Structure of a protein from Haloferax volcanii.";
RL Submitted (SEP-2011) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF GLU-53.
RC STRAIN=DS2;
RX PubMed=23821306; DOI=10.1002/pro.2305;
RA Li Y., Maciejewski M.W., Martin J., Jin K., Zhang Y., Maupin-Furlow J.A.,
RA Hao B.;
RT "Crystal structure of the ubiquitin-like small archaeal modifier protein 2
RT from Haloferax volcanii.";
RL Protein Sci. 22:1206-1217(2013).
CC -!- FUNCTION: Functions as a protein modifier covalently attached to lysine
CC residues of substrate proteins, as well as a sulfur carrier in tRNA
CC thiolation. The protein modification process is termed sampylation and
CC involves the formation of an isopeptide bond between the SAMP2 C-
CC terminal glycine carboxylate and the epsilon-amino group of lysine
CC residues on target proteins. Is able to form polymeric chains with
CC itself at Lys-58, similar to ubiquitin and other ubiquitin-like
CC proteins. May serve as a proteolytic signal in the cell to target
CC proteins for degradation by proteasomes. {ECO:0000269|PubMed:20054389,
CC ECO:0000269|PubMed:21368171, ECO:0000269|PubMed:24097257}.
CC -!- SUBUNIT: Monomer (PubMed:23821306). Monomeric and polymeric forms
CC interact with NcsA (PubMed:24906001). {ECO:0000269|PubMed:23821306,
CC ECO:0000269|PubMed:24906001}.
CC -!- PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA,
CC and also probably thiocarboxylated (-COSH) to function in sulfur
CC transfer. {ECO:0000269|PubMed:21368171}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow similarly to wild-
CC type in the presence of either DMSO or oxygen as the terminal electron
CC acceptor, but are retarded in aerobic growth at 50 degrees Celsius. The
CC lysine tRNAs of the mutant strain appear to be nonthiolated.
CC {ECO:0000269|PubMed:21368171}.
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DR EMBL; CP001956; ADE03392.1; -; Genomic_DNA.
DR RefSeq; WP_004045316.1; NZ_AOHU01000106.1.
DR PDB; 2L32; NMR; -; A=1-66.
DR PDB; 2LJI; NMR; -; A=1-66.
DR PDB; 4HRS; X-ray; 2.30 A; A=2-66.
DR PDBsum; 2L32; -.
DR PDBsum; 2LJI; -.
DR PDBsum; 4HRS; -.
DR AlphaFoldDB; D4GZE7; -.
DR BMRB; D4GZE7; -.
DR SMR; D4GZE7; -.
DR STRING; 309800.C498_19264; -.
DR EnsemblBacteria; ADE03392; ADE03392; HVO_0202.
DR GeneID; 8926718; -.
DR KEGG; hvo:HVO_0202; -.
DR eggNOG; arCOG00535; Archaea.
DR HOGENOM; CLU_114601_9_3_2; -.
DR OMA; AGYHPQE; -.
DR OrthoDB; 127668at2157; -.
DR EvolutionaryTrace; D4GZE7; -.
DR Proteomes; UP000008243; Chromosome.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0031386; F:protein tag; IDA:UniProtKB.
DR GO; GO:0032446; P:protein modification by small protein conjugation; IDA:UniProtKB.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR SUPFAM; SSF54285; SSF54285; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isopeptide bond; Nucleotide-binding; Phosphoprotein;
KW Reference proteome; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..66
FT /note="Small archaeal modifier protein 2"
FT /id="PRO_0000397102"
FT MOD_RES 66
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000269|PubMed:21368171"
FT MOD_RES 66
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000269|PubMed:21368171"
FT CROSSLNK 58
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SAMP2)"
FT CROSSLNK 66
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins); alternate"
FT MUTAGEN 53
FT /note="E->G: Abolishes SAMPylation of substrate proteins."
FT /evidence="ECO:0000269|PubMed:23821306"
FT MUTAGEN 58
FT /note="K->R: Loss of isopeptide linkage of polymeric chains
FT on NcsA; when associated with R-64."
FT /evidence="ECO:0000269|PubMed:24906001"
FT MUTAGEN 64
FT /note="K->R: Loss of isopeptide linkage of polymeric chains
FT on NcsA; when associated with R-58."
FT /evidence="ECO:0000269|PubMed:24906001"
FT MUTAGEN 65..66
FT /note="Missing: Abolishes SAMPylation of substrate
FT proteins."
FT /evidence="ECO:0000269|PubMed:20054389"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:4HRS"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:4HRS"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:4HRS"
FT HELIX 34..36
FT /evidence="ECO:0007829|PDB:4HRS"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:4HRS"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:4HRS"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:2LJI"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:4HRS"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:2L32"
SQ SEQUENCE 66 AA; 7118 MW; 09442B0B845C7DE0 CRC64;
MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ SVEVDRVKVL
RLIKGG
