ID   SAMP3_HALVD             Reviewed;          92 AA.
AC   D4GVB0;
DT   14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT   14-MAY-2014, sequence version 2.
DT   25-MAY-2022, entry version 50.
DE   RecName: Full=Small archaeal modifier protein 3;
DE            Short=SAMP3;
DE   AltName: Full=Ubiquitin-like small archaeal modifier protein 3;
GN   Name=samp3; OrderedLocusNames=HVO_2177;
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, AMPYLATION AT GLY-92, 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   [3]
RP   FUNCTION AS A PROTEIN MODIFIER, PROTEIN TARGETS, CROSS-LINK, INDUCTION,
RP   MUTAGENESIS OF 91-GLY-GLY-92, AND IDENTIFICATION OF START SITE.
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   [4]
RP   STRUCTURE BY NMR, AND SUBUNIT.
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. The protein modification process is
CC       termed sampylation and involves the formation of an isopeptide bond
CC       between the SAMP3 C-terminal glycine carboxylate and the epsilon-amino
CC       group of lysine residues on target proteins. Seems to be able to form
CC       polymeric chains with itself at Lys-18, Lys-55 and Lys-62, similar to
CC       ubiquitin and other ubiquitin-like proteins. SAMP3 appears not to serve
CC       as a proteolytic signal in the cell to target proteins for degradation
CC       by proteasomes. May regulate molybdenum cofactor (MoCo) biosynthesis by
CC       inhibiting the activity of MPT synthase MoaE under aerobic conditions,
CC       providing a hierarchy of oxygen use prior to that of alternative
CC       electron acceptors such as DMSO. {ECO:0000269|PubMed:21368171,
CC       ECO:0000269|PubMed:24097257}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:23821306}.
CC   -!- INDUCTION: Up-regulated by the addition of dimethyl sulfoxide to
CC       aerobically growing cells. These conditions also increase the levels of
CC       SAMP3 conjugates in cells. {ECO:0000269|PubMed:24097257}.
CC   -!- PTM: The C-terminal glycine is likely acyl-adenylated (-COAMP) by UbaA.
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; thus, SAMP3 is not needed for DMSO respiration, suggesting
CC       that it is not required for molybdenum cofactor (MoCo) biosynthesis.
CC       tRNA thiolation is not affected. {ECO:0000269|PubMed:21368171}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADE02783.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; CP001956; ADE02783.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004042069.1; NZ_AOHU01000041.1.
DR   PDB; 2M19; NMR; -; A=1-92.
DR   PDBsum; 2M19; -.
DR   AlphaFoldDB; D4GVB0; -.
DR   BMRB; D4GVB0; -.
DR   SMR; D4GVB0; -.
DR   STRING; 309800.C498_06178; -.
DR   EnsemblBacteria; ADE02783; ADE02783; HVO_2177.
DR   GeneID; 8923994; -.
DR   KEGG; hvo:HVO_2177; -.
DR   eggNOG; arCOG00536; Archaea.
DR   HOGENOM; CLU_114601_1_2_2; -.
DR   OrthoDB; 119587at2157; -.
DR   Proteomes; UP000008243; Chromosome.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.20.30; -; 1.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR010038; MoaD_arc-typ.
DR   InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR   InterPro; IPR003749; ThiS/MoaD-like.
DR   Pfam; PF02597; ThiS; 1.
DR   SUPFAM; SSF54285; SSF54285; 1.
DR   TIGRFAMs; TIGR01687; moaD_arch; 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..92
FT                   /note="Small archaeal modifier protein 3"
FT                   /id="PRO_0000428940"
FT   MOD_RES         92
FT                   /note="Glycyl adenylate; alternate"
FT                   /evidence="ECO:0000269|PubMed:21368171"
FT   CROSSLNK        18
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP3)"
FT   CROSSLNK        55
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP3)"
FT   CROSSLNK        62
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SAMP3)"
FT   CROSSLNK        92
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins); alternate"
FT   MUTAGEN         91..92
FT                   /note="Missing: Abolishes conjugation of SAMP3 to protein
FT                   targets."
FT                   /evidence="ECO:0000269|PubMed:24097257"
FT   STRAND          1..7
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   HELIX           10..15
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   STRAND          18..25
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   HELIX           30..40
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   HELIX           42..44
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   TURN            45..48
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   STRAND          59..62
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   STRAND          72..75
FT                   /evidence="ECO:0007829|PDB:2M19"
FT   STRAND          82..86
FT                   /evidence="ECO:0007829|PDB:2M19"
SQ   SEQUENCE   92 AA;  10046 MW;  425F8EA3DE9904A3 CRC64;
     MELELRFFAT FREVVGQKSI YWRVDDDATV GDVLRSLEAE YDGLAGRLIE DGEVKPHVNV
     LKNGREVVHL DGMATALDDG DAVSVFPPVA GG