SAMP1_HALVD
ID SAMP1_HALVD Reviewed; 87 AA.
AC D4GUF6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=Small archaeal modifier protein 1;
DE Short=SAMP1;
DE AltName: Full=Ubiquitin-like small archaeal modifier protein 1;
GN Name=samp1; OrderedLocusNames=HVO_2619;
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, AND MUTAGENESIS OF 86-GLY-GLY-87.
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-87, AMPYLATION AT GLY-87, 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, AND CROSS-LINK.
RC STRAIN=DS2 / DS70;
RX PubMed=22970855; DOI=10.1111/mmi.12038;
RA Hepowit N.L., Uthandi S., Miranda H.V., Toniutti M., Prunetti L.,
RA Olivarez O., De Vera I.M., Fanucci G.E., Chen S., Maupin-Furlow J.A.;
RT "Archaeal JAB1/MPN/MOV34 metalloenzyme (HvJAMM1) cleaves ubiquitin-like
RT small archaeal modifier proteins (SAMPs) from protein-conjugates.";
RL Mol. Microbiol. 86:971-987(2012).
RN [6]
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 [7]
RP STRUCTURE BY NMR.
RA Zhang W., Liao S., Fan K., Zhang J., Tu X.;
RT "A protein from Haloferax volcanii.";
RL Submitted (JAN-2011) to the PDB data bank.
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS).
RX PubMed=21216237; DOI=10.1016/j.bbrc.2011.01.004;
RA Jeong Y.J., Jeong B.C., Song H.K.;
RT "Crystal structure of ubiquitin-like small archaeal modifier protein 1
RT (SAMP1) from Haloferax volcanii.";
RL Biochem. Biophys. Res. Commun. 405:112-117(2011).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.15 ANGSTROMS).
RA Li Y., Maciejewski M.W., Jin K., Martin J., Zhang Y., Lu M.,
RA Maupin-Furlow J.A., Hao B.;
RT "Crystal structure of H.volcanii small archaeal modifier protein 1.";
RL Submitted (OCT-2012) to the PDB data bank.
CC -!- FUNCTION: Functions as a protein modifier covalently attached to lysine
CC residues of substrate proteins, as well as a sulfur carrier in
CC molybdenum cofactor (MoCo) biosynthesis. The protein modification
CC process is termed sampylation and involves the formation of an
CC isopeptide bond between the SAMP1 C-terminal glycine carboxylate and
CC the epsilon-amino group of lysine residues on target proteins. May
CC serve as a proteolytic signal in the cell to target proteins for
CC degradation by proteasomes. {ECO:0000269|PubMed:20054389,
CC ECO:0000269|PubMed:21368171, ECO:0000269|PubMed:22970855,
CC ECO:0000269|PubMed:24097257}.
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 do not grow anaerobically
CC with DMSO and do not show DMSO reductase activity, but their growth in
CC the presence of oxygen and at 50 degrees Celsius is not affected. SAMP2
CC and SAMP3 cannot complement the samp1 mutation. tRNA thiolation is not
CC affected. {ECO:0000269|PubMed:21368171}.
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DR EMBL; CP001956; ADE04519.1; -; Genomic_DNA.
DR RefSeq; WP_004042720.1; NZ_AOHU01000046.1.
DR PDB; 2L83; NMR; -; A=1-87.
DR PDB; 3PO0; X-ray; 1.55 A; A=1-87.
DR PDB; 4HRO; X-ray; 1.15 A; A/B=1-87.
DR PDBsum; 2L83; -.
DR PDBsum; 3PO0; -.
DR PDBsum; 4HRO; -.
DR AlphaFoldDB; D4GUF6; -.
DR BMRB; D4GUF6; -.
DR SMR; D4GUF6; -.
DR STRING; 309800.C498_08375; -.
DR EnsemblBacteria; ADE04519; ADE04519; HVO_2619.
DR GeneID; 8925082; -.
DR KEGG; hvo:HVO_2619; -.
DR eggNOG; arCOG00536; Archaea.
DR HOGENOM; CLU_114601_1_2_2; -.
DR OMA; TEWKLFA; -.
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_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 pathway.
FT CHAIN 1..87
FT /note="Small archaeal modifier protein 1"
FT /id="PRO_0000397101"
FT MOD_RES 87
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000269|PubMed:21368171"
FT MOD_RES 87
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000269|PubMed:21368171"
FT CROSSLNK 87
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins); alternate"
FT MUTAGEN 86..87
FT /note="Missing: Abolishes sampylation of substrate
FT proteins."
FT /evidence="ECO:0000269|PubMed:20054389"
FT STRAND 1..5
FT /evidence="ECO:0007829|PDB:4HRO"
FT HELIX 7..13
FT /evidence="ECO:0007829|PDB:4HRO"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:4HRO"
FT HELIX 28..38
FT /evidence="ECO:0007829|PDB:4HRO"
FT HELIX 40..42
FT /evidence="ECO:0007829|PDB:4HRO"
FT HELIX 43..46
FT /evidence="ECO:0007829|PDB:4HRO"
FT STRAND 58..61
FT /evidence="ECO:0007829|PDB:4HRO"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:4HRO"
SQ SEQUENCE 87 AA; 8937 MW; B06496AD43000BFF CRC64;
MEWKLFADLA EVAGSRTVRV DVDGDATVGD ALDALVGAHP ALESRVFGDD GELYDHINVL
RNGEAAALGE ATAAGDELAL FPPVSGG
