DBH_THET8
ID DBH_THET8 Reviewed; 96 AA.
AC P19436; Q5SIM0;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 29-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=DNA-binding protein HU;
DE AltName: Full=DNA-binding protein II;
DE AltName: Full=TL29;
GN OrderedLocusNames=TTHA1349;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP PROTEIN SEQUENCE.
RX PubMed=2226865; DOI=10.1016/0014-5793(90)81050-x;
RA Zierer R., Choli D.;
RT "The primary structure of DNA binding protein II from the extreme
RT thermophilic bacterium Thermus thermophilus.";
RL FEBS Lett. 273:59-62(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP PROTEIN SEQUENCE OF 1-59, AND ISOLATION OF 5S RRNA-ASSOCIATED COMPLEXES.
RA Kim J.-S., Boysen R.I., Schroeder W., Erdmann V.A., Gessner R.V.;
RT "Identification, pruification and partial sequence of four Thermus
RT thermophilus 5S rRNA binding proteins.";
RL Endocyt. Cell Res. 11:177-194(1996).
CC -!- FUNCTION: Histone-like DNA-binding protein which is capable of wrapping
CC DNA to stabilize it, and thus to prevent its denaturation under extreme
CC environmental conditions.
CC -!- SUBUNIT: Has been isolated as a complex with 5S rRNA and RL25, 5S rRNA,
CC RL25 and RL5. Homodimer.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; AP008226; BAD71172.1; -; Genomic_DNA.
DR RefSeq; YP_144615.1; NC_006461.1.
DR PDB; 5EKA; X-ray; 1.69 A; A=1-96.
DR PDBsum; 5EKA; -.
DR AlphaFoldDB; P19436; -.
DR SMR; P19436; -.
DR STRING; 300852.55772731; -.
DR EnsemblBacteria; BAD71172; BAD71172; BAD71172.
DR KEGG; ttj:TTHA1349; -.
DR PATRIC; fig|300852.9.peg.1326; -.
DR eggNOG; COG0776; Bacteria.
DR HOGENOM; CLU_105066_3_1_0; -.
DR OMA; PAHEGIN; -.
DR Proteomes; UP000000532; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR Gene3D; 4.10.520.10; -; 1.
DR InterPro; IPR000119; Hist_DNA-bd.
DR InterPro; IPR020816; Histone-like_DNA-bd_CS.
DR InterPro; IPR010992; IHF-like_DNA-bd_dom_sf.
DR PANTHER; PTHR33175; PTHR33175; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR PRINTS; PR01727; DNABINDINGHU.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; SSF47729; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; DNA condensation; DNA-binding;
KW Reference proteome.
FT CHAIN 1..96
FT /note="DNA-binding protein HU"
FT /id="PRO_0000104990"
FT CONFLICT 8
FT /note="K -> L (in Ref. 3; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 23..24
FT /note="KK -> LL (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 8..19
FT /evidence="ECO:0007829|PDB:5EKA"
FT HELIX 23..42
FT /evidence="ECO:0007829|PDB:5EKA"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5EKA"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:5EKA"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:5EKA"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:5EKA"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:5EKA"
SQ SEQUENCE 96 AA; 10321 MW; F5E0E08895EF35FC CRC64;
AAKKTVTKAD LVDQVAQATG LKKKDVKAMV DALLAKVEEA LANGSKVQLT GFGTFEVRKR
KARTGVKPGT KEKIKIPATQ YPAFKPGKAL KDKVKK
