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 23-FEB-2022, entry version 56. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 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; MHVTVDV; -. 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 //