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   27-MAR-2024, entry version 62.
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 /
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., 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 /
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., 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   AlphaFoldDB; D4GZE7; -.
DR   BMRB; D4GZE7; -.
DR   SMR; D4GZE7; -.
DR   STRING; 309800.HVO_0202; -.
DR   PaxDb; 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   OrthoDB; 104640at2157; -.
DR   EvolutionaryTrace; D4GZE7; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0031386; F:protein tag activity; IDA:UniProtKB.
DR   GO; GO:0032446; P:protein modification by small protein conjugation; IDA:UniProtKB.
DR   Gene3D; 4.10.410.50; -; 1.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   NCBIfam; NF041919; SAMP2; 1.
DR   SUPFAM; SSF54285; MoaD/ThiS; 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
//