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 04-MAR-2015, entry version 34. 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 OS 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii). OC Archaea; Euryarchaeota; Halobacteria; Halobacteriales; OC Halobacteriaceae; 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 / RC VKM 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., RA Madupu R., Robinson J., Khouri H., Ren Q., Lowe T.M., RA Maupin-Furlow J., Pohlschroder M., Daniels C., Pfeiffer F., Allers T., RA 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, RP SAMPYLATION AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY, AND RP MUTAGENESIS OF 65-GLY-GLY-66. RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / RC VKM 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., RA Zhou G., 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, AND DISRUPTION 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 RT UbaA-dependent mechanism."; RL Mol. Cell. Proteomics 13:220-239(2014). RN [6] RP STRUCTURE BY NMR. RA Fan S., Zhang W., Liao S., Tu X.; RT "Solution structure of ubiquitin-like small archaeal modifier protein RT in Haloferax volcanii."; RL Submitted (SEP-2010) to the PDB data bank. RN [7] 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 [8] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS), SUBUNIT, AND MUTAGENESIS OF RP 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., RA Maupin-Furlow J.A., Hao B.; RT "Crystal structure of the ubiquitin-like small archaeal modifier RT protein 2 from Haloferax volcanii."; RL Protein Sci. 22:1206-1217(2013). CC -!- FUNCTION: Functions as a protein modifier covalently attached to CC lysine residues of substrate proteins, as well as a sulfur carrier CC in tRNA thiolation. The protein modification process is termed CC sampylation and involves the formation of an isopeptide bond CC between the SAMP2 C-terminal glycine carboxylate and the epsilon- CC amino group of lysine residues on target proteins. Is able to form CC polymeric chains with itself at Lys-58, similar to ubiquitin and CC other ubiquitin-like proteins. May serve as a proteolytic signal CC in the cell to target proteins for degradation by proteasomes. CC {ECO:0000269|PubMed:20054389, ECO:0000269|PubMed:21368171, CC ECO:0000269|PubMed:24097257}. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23821306}. CC -!- PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by CC UbaA, and also probably thiocarboxylated (-COSH) to function in CC sulfur transfer. {ECO:0000269|PubMed:21368171}. CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene grow similarly to CC wild-type in the presence of either DMSO or oxygen as the terminal CC electron acceptor, but are retarded in aerobic growth at 50 CC degrees Celsius. The lysine tRNAs of the mutant strain appear to CC be nonthiolated. {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 RefSeq; YP_003534279.1; NC_013967.1. 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 EnsemblBacteria; ADE03392; ADE03392; HVO_0202. DR GeneID; 8926718; -. DR KEGG; hvo:HVO_0202; -. DR HOGENOM; HOG000227894; -. DR KO; K03154; -. DR OMA; PEDQPVE; -. DR BioCyc; HVOL309800:GCOK-206-MONOMER; -. 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 Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b. DR SUPFAM; SSF54285; SSF54285; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isopeptide bond; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Ubl conjugation; KW Ubl conjugation pathway. FT CHAIN 1 66 Small archaeal modifier protein 2. FT /FTId=PRO_0000397102. FT MOD_RES 66 66 1-thioglycine; alternate. {ECO:0000305}. FT MOD_RES 66 66 Glycyl adenylate; alternate. FT {ECO:0000305}. FT CROSSLNK 58 58 Glycyl lysine isopeptide (Lys-Gly) FT (interchain with G-Cter in SAMP2). FT CROSSLNK 66 66 Glycyl lysine isopeptide (Gly-Lys) FT (interchain with K-? in acceptor FT proteins); alternate. FT MUTAGEN 53 53 E->G: Abolishes SAMPylation of substrate FT proteins. {ECO:0000269|PubMed:23821306}. FT MUTAGEN 65 66 Missing: Abolishes SAMPylation of FT substrate proteins. FT {ECO:0000269|PubMed:20054389}. FT STRAND 2 6 {ECO:0000244|PDB:4HRS}. FT STRAND 12 16 {ECO:0000244|PDB:4HRS}. FT HELIX 23 29 {ECO:0000244|PDB:4HRS}. FT HELIX 34 36 {ECO:0000244|PDB:4HRS}. FT STRAND 39 41 {ECO:0000244|PDB:4HRS}. FT STRAND 44 46 {ECO:0000244|PDB:4HRS}. FT HELIX 47 49 {ECO:0000244|PDB:2LJI}. FT STRAND 50 53 {ECO:0000244|PDB:4HRS}. FT STRAND 57 59 {ECO:0000244|PDB:2L32}. SQ SEQUENCE 66 AA; 7118 MW; 09442B0B845C7DE0 CRC64; MNVTVEVVGE ETSEVAVDDD GTYADLVRAV DLSPHEVTVL VDGRPVPEDQ SVEVDRVKVL RLIKGG //