DN7D_SULAC
ID DN7D_SULAC Reviewed; 66 AA.
AC P13123; Q4JCI7;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 25-MAY-2022, entry version 140.
DE RecName: Full=DNA-binding protein 7d {ECO:0000305};
DE AltName: Full=7 kDa DNA-binding protein d;
DE AltName: Full=Sac7d;
DE Contains:
DE RecName: Full=DNA-binding protein 7a;
DE AltName: Full=7 kDa DNA-binding protein a;
DE AltName: Full=Sac7a;
DE Contains:
DE RecName: Full=DNA-binding protein 7b;
DE AltName: Full=7 kDa DNA-binding protein b;
DE AltName: Full=Sac7b;
GN OrderedLocusNames=Saci_0064;
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DNA-BINDING.
RX PubMed=7632679; DOI=10.1021/bi00031a031;
RA McAfee J.G., Edmondson S.P., Datta P.K., Shriver J.W., Gupta R.;
RT "Gene cloning, expression, and characterization of the Sac7 proteins from
RT the hyperthermophile Sulfolobus acidocaldarius.";
RL Biochemistry 34:10063-10077(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [3]
RP PROTEIN SEQUENCE OF 2-65.
RX PubMed=6436055; DOI=10.1016/0014-5793(84)80935-7;
RA Kimura M., Kimura J., Davie P., Reinhardt R., Dijk J.;
RT "The amino acid sequence of a small DNA binding protein from the
RT archaebacterium Sulfolobus solfataricus.";
RL FEBS Lett. 176:176-178(1984).
RN [4]
RP PROTEIN SEQUENCE OF 2-62, AND METHYLATION AT LYS-5 AND LYS-7.
RX PubMed=3130377; DOI=10.1016/s0021-9258(18)68608-9;
RA Choli T., Wittmann-Liebold B., Reinhardt R.;
RT "Microsequence analysis of DNA-binding proteins 7a, 7b, and 7e from the
RT archaebacterium Sulfolobus acidocaldarius.";
RL J. Biol. Chem. 263:7087-7093(1988).
RN [5]
RP DNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR
RP LOCATION.
RX PubMed=27853299; DOI=10.1038/srep37274;
RA Kalichuk V., Behar G., Renodon-Corniere A., Danovski G., Obal G.,
RA Barbet J., Mouratou B., Pecorari F.;
RT "The archaeal '7 kDa DNA-binding' proteins: extended characterization of an
RT old gifted family.";
RL Sci. Rep. 6:37274-37274(2016).
RN [6]
RP STRUCTURE BY NMR.
RX PubMed=7577913; DOI=10.1021/bi00041a004;
RA Edmondson S.P., Qiu L., Shriver J.W.;
RT "Solution structure of the DNA-binding protein Sac7d from the
RT hyperthermophile Sulfolobus acidocaldarius.";
RL Biochemistry 34:13289-13304(1995).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND DNA-BINDING.
RX PubMed=9515968; DOI=10.1038/32455;
RA Robinson H., Gao Y.-G., McCrary B.S., Edmondson S.P., Shriver J.W.,
RA Wang A.H.-J.;
RT "The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.";
RL Nature 392:202-205(1998).
CC -!- FUNCTION: Can constrain negative DNA supercoils. May be involved in
CC maintaining the integrity of the genome at high temperature.
CC {ECO:0000250|UniProtKB:P61990}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Highly stable from pH 0 to pH 12. {ECO:0000269|PubMed:27853299};
CC Temperature dependence:
CC Hyperthermostable. {ECO:0000269|PubMed:27853299};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27853299}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27853299}.
CC -!- PTM: Lys-5 was 70% monomethylated in form 7a, 25% in form 7b, and 20%
CC in form 7d. Lys-7 was 50% monomethylated in form 7a, 40% in form 7b,
CC and 50% in form 7d. {ECO:0000269|PubMed:3130377}.
CC -!- MISCELLANEOUS: Sac7a and Sac7b are truncated versions of the Sac7d
CC protein, most likely resulting from post-translational processing, or
CC degradation during isolation. {ECO:0000305|PubMed:7632679}.
CC -!- SIMILARITY: Belongs to the 7 kDa DNA-binding/endoribonuclease P2
CC family. {ECO:0000305}.
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DR EMBL; M87569; AAA80315.1; -; Genomic_DNA.
DR EMBL; CP000077; AAY79492.1; -; Genomic_DNA.
DR PIR; A27749; A27749.
DR RefSeq; WP_011276993.1; NC_007181.1.
DR PDB; 1AZP; X-ray; 1.60 A; A=1-66.
DR PDB; 1AZQ; X-ray; 1.94 A; A=1-66.
DR PDB; 1BF4; X-ray; 1.60 A; A=4-66.
DR PDB; 1CA5; X-ray; 2.20 A; A=1-66.
DR PDB; 1CA6; X-ray; 2.20 A; A=1-66.
DR PDB; 1SAP; NMR; -; A=1-66.
DR PDB; 1WD0; X-ray; 1.90 A; A=1-66.
DR PDB; 1WD1; X-ray; 2.20 A; A=1-66.
DR PDB; 1WTO; X-ray; 1.50 A; A=1-66.
DR PDB; 1WTP; X-ray; 1.90 A; A/B=1-66.
DR PDB; 1WTQ; X-ray; 1.70 A; A=1-66.
DR PDB; 1WTR; X-ray; 1.80 A; A=1-66.
DR PDB; 1WTV; X-ray; 1.60 A; A=1-66.
DR PDB; 1WTW; X-ray; 2.20 A; A=1-66.
DR PDB; 1WTX; X-ray; 2.20 A; A=1-66.
DR PDB; 1WVL; X-ray; 2.60 A; A/B=1-66.
DR PDB; 1XX8; NMR; -; A=1-66.
DR PDB; 1XYI; X-ray; 1.45 A; A=1-66.
DR PDB; 2XIW; X-ray; 1.50 A; A/B=2-66.
DR PDB; 4CJ1; X-ray; 1.63 A; B=2-62.
DR PDB; 4CJ2; X-ray; 1.50 A; C/D=2-66.
DR PDBsum; 1AZP; -.
DR PDBsum; 1AZQ; -.
DR PDBsum; 1BF4; -.
DR PDBsum; 1CA5; -.
DR PDBsum; 1CA6; -.
DR PDBsum; 1SAP; -.
DR PDBsum; 1WD0; -.
DR PDBsum; 1WD1; -.
DR PDBsum; 1WTO; -.
DR PDBsum; 1WTP; -.
DR PDBsum; 1WTQ; -.
DR PDBsum; 1WTR; -.
DR PDBsum; 1WTV; -.
DR PDBsum; 1WTW; -.
DR PDBsum; 1WTX; -.
DR PDBsum; 1WVL; -.
DR PDBsum; 1XX8; -.
DR PDBsum; 1XYI; -.
DR PDBsum; 2XIW; -.
DR PDBsum; 4CJ1; -.
DR PDBsum; 4CJ2; -.
DR AlphaFoldDB; P13123; -.
DR BMRB; P13123; -.
DR SMR; P13123; -.
DR iPTMnet; P13123; -.
DR EnsemblBacteria; AAY79492; AAY79492; Saci_0064.
DR GeneID; 3473894; -.
DR KEGG; sai:Saci_0064; -.
DR PATRIC; fig|330779.12.peg.59; -.
DR eggNOG; arCOG05888; Archaea.
DR HOGENOM; CLU_2929990_0_0_2; -.
DR OMA; MATKIKF; -.
DR EvolutionaryTrace; P13123; -.
DR Proteomes; UP000001018; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR003212; DNA-bd_7kDa_arc.
DR Pfam; PF02294; 7kD_DNA_binding; 1.
DR PIRSF; PIRSF036912; Sac7; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Methylation; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3130377,
FT ECO:0000269|PubMed:6436055"
FT CHAIN 2..65
FT /note="DNA-binding protein 7d"
FT /id="PRO_0000007248"
FT CHAIN 2..62
FT /note="DNA-binding protein 7a"
FT /id="PRO_0000007249"
FT CHAIN 2..59
FT /note="DNA-binding protein 7b"
FT /id="PRO_0000007250"
FT MOD_RES 5
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:3130377"
FT MOD_RES 7
FT /note="N6-methyllysine; partial"
FT /evidence="ECO:0000269|PubMed:3130377"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:1XYI"
FT STRAND 11..16
FT /evidence="ECO:0007829|PDB:1XYI"
FT HELIX 17..19
FT /evidence="ECO:0007829|PDB:1XYI"
FT STRAND 20..26
FT /evidence="ECO:0007829|PDB:1XYI"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:1XYI"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:1XYI"
FT HELIX 47..49
FT /evidence="ECO:0007829|PDB:1XYI"
FT HELIX 52..62
FT /evidence="ECO:0007829|PDB:1XYI"
SQ SEQUENCE 66 AA; 7609 MW; BFF84F058C2DDA97 CRC64;
MVKVKFKYKG EEKEVDTSKI KKVWRVGKMV SFTYDDNGKT GRGAVSEKDA PKELLDMLAR
AEREKK
