SAMP2_PYRFU
ID SAMP2_PYRFU Reviewed; 69 AA.
AC Q8U1Z3;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 91.
DE RecName: Full=Small archaeal modifier protein 2 {ECO:0000303|PubMed:28479062};
DE Short=SAMP2 {ECO:0000303|PubMed:28479062};
DE AltName: Full=Ubiquitin-like small archaeal modifier protein 2 {ECO:0000303|PubMed:28479062};
GN Name=samp2 {ECO:0000303|PubMed:28479062};
GN OrderedLocusNames=PF1061 {ECO:0000312|EMBL:AAL81185.1};
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1
RC {ECO:0000312|Proteomes:UP000001013};
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2] {ECO:0007744|PDB:1RWS, ECO:0007744|PDB:1SF0}
RP STRUCTURE BY NMR OF 2-69.
RX PubMed=15704012; DOI=10.1007/s10969-005-4899-5;
RA Valafar H., Mayer K.L., Bougault C.M., LeBlond P.D., Jenney F.E.,
RA Brereton P.S., Adams M.W., Prestegard J.H.;
RT "Backbone solution structures of proteins using residual dipolar couplings:
RT application to a novel structural genomics target.";
RL J. Struct. Funct. Genomics 5:241-254(2004).
RN [3] {ECO:0007744|PDB:5LDA}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH PFJAMM1 PROTEIN, AND
RP FUNCTION.
RX PubMed=28479062; DOI=10.1016/j.str.2017.04.002;
RA Cao S., Engilberge S., Girard E., Gabel F., Franzetti B.,
RA Maupin-Furlow J.A.;
RT "Structural insight into ubiquitin-like protein recognition and oligomeric
RT states of JAMM/MPN+ proteases.";
RL Structure 25:823-833(2017).
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 likely at Lys-55, 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:0000250|UniProtKB:D4GZE7,
CC ECO:0000305|PubMed:15704012}.
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:0000250|UniProtKB:D4GZE7}.
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DR EMBL; AE009950; AAL81185.1; -; Genomic_DNA.
DR PDB; 1RWS; NMR; -; A=2-69.
DR PDB; 1SF0; NMR; -; A=2-69.
DR PDB; 5LDA; X-ray; 1.90 A; B=1-69.
DR PDBsum; 1RWS; -.
DR PDBsum; 1SF0; -.
DR PDBsum; 5LDA; -.
DR AlphaFoldDB; Q8U1Z3; -.
DR SMR; Q8U1Z3; -.
DR STRING; 186497.PF1061; -.
DR EnsemblBacteria; AAL81185; AAL81185; PF1061.
DR KEGG; pfu:PF1061; -.
DR PATRIC; fig|186497.12.peg.1122; -.
DR eggNOG; arCOG00535; Archaea.
DR HOGENOM; CLU_114601_9_4_2; -.
DR OMA; IEWREGM; -.
DR PhylomeDB; Q8U1Z3; -.
DR EvolutionaryTrace; Q8U1Z3; -.
DR Proteomes; UP000001013; 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; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR003749; ThiS/MoaD-like.
DR Pfam; PF02597; ThiS; 1.
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..69
FT /note="Small archaeal modifier protein 2"
FT /id="PRO_0000441761"
FT MOD_RES 69
FT /note="1-thioglycine; alternate"
FT /evidence="ECO:0000250|UniProtKB:D4GZE7"
FT MOD_RES 69
FT /note="Glycyl adenylate; alternate"
FT /evidence="ECO:0000250|UniProtKB:D4GZE7"
FT CROSSLNK 55
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SAMP2)"
FT /evidence="ECO:0000250|UniProtKB:D4GZE7"
FT CROSSLNK 69
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins); alternate"
FT /evidence="ECO:0000250|UniProtKB:D4GZE7"
FT STRAND 6..8
FT /evidence="ECO:0007829|PDB:5LDA"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:5LDA"
FT HELIX 25..31
FT /evidence="ECO:0007829|PDB:5LDA"
FT TURN 36..38
FT /evidence="ECO:0007829|PDB:5LDA"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:5LDA"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:5LDA"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:1RWS"
FT STRAND 60..64
FT /evidence="ECO:0007829|PDB:5LDA"
SQ SEQUENCE 69 AA; 7686 MW; BFDE8FF3EE8A7F15 CRC64;
MKMIKVKVIG RNIEKEIEWR EGMKVRDILR AVGFNTESAI AKVNGKVVLE DDEVKDGDFV
EVIPVVSGG
