DBH_GEOSE
ID DBH_GEOSE Reviewed; 90 AA.
AC P0A3H0; P02346; P08822;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=DNA-binding protein HU;
DE AltName: Full=DNA-binding protein II;
DE AltName: Full=HB;
GN Name=hup; Synonyms=hbs, hbsU;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1644313; DOI=10.1016/0378-1119(92)90487-a;
RA Padas P.M., Wilson K.S., Vorgias C.E.;
RT "The DNA-binding protein HU from mesophilic and thermophilic bacilli: gene
RT cloning, overproduction and purification.";
RL Gene 117:39-44(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1503;
RX PubMed=7765961; DOI=10.1271/bbb.59.126;
RA Kawamura S., Kajiyama H., Yamasaki N., Kimura M.;
RT "Cloning of the gene encoding DNA binding protein HU from Bacillus
RT stearothermophilus and its expression in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 59:126-129(1995).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=6300069; DOI=10.1016/s0021-9258(18)32768-6;
RA Kimura M., Wilson K.S.;
RT "On the DNA binding protein II from Bacillus stearothermophilus. II. The
RT amino acid sequence and its relation to those of homologous proteins from
RT other prokaryotes.";
RL J. Biol. Chem. 258:4007-4011(1983).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3 ANGSTROMS).
RX PubMed=6540370; DOI=10.1038/310376a0;
RA Tanaka I., Appelt K., Dijk J., White S.W., Wilson K.S.;
RT "3-A resolution structure of a protein with histone-like properties in
RT prokaryotes.";
RL Nature 310:376-381(1984).
RN [5]
RP STRUCTURE BY NMR.
RX PubMed=7500343; DOI=10.1006/jmbi.1995.0648;
RA Vis H., Mariani M., Vorgias C.E., Wilson K.S., Kaptein R., Boelens R.;
RT "Solution structure of the HU protein from Bacillus stearothermophilus.";
RL J. Mol. Biol. 254:692-703(1995).
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: Homodimer.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; M73500; AAA22532.1; -; Genomic_DNA.
DR EMBL; D38080; BAA07273.1; -; Genomic_DNA.
DR PIR; JC1205; DNBS2F.
DR PDB; 1HUE; NMR; -; A/B=1-90.
DR PDB; 1HUU; X-ray; 2.00 A; A/B/C=1-90.
DR PDBsum; 1HUE; -.
DR PDBsum; 1HUU; -.
DR AlphaFoldDB; P0A3H0; -.
DR BMRB; P0A3H0; -.
DR SMR; P0A3H0; -.
DR PRIDE; P0A3H0; -.
DR EvolutionaryTrace; P0A3H0; -.
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 Phosphoprotein.
FT CHAIN 1..90
FT /note="DNA-binding protein HU"
FT /id="PRO_0000104912"
FT REGION 56..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250"
FT HELIX 3..14
FT /evidence="ECO:0007829|PDB:1HUU"
FT HELIX 18..37
FT /evidence="ECO:0007829|PDB:1HUU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:1HUU"
FT TURN 45..47
FT /evidence="ECO:0007829|PDB:1HUU"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1HUU"
FT STRAND 59..61
FT /evidence="ECO:0007829|PDB:1HUE"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:1HUE"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1HUU"
FT HELIX 83..89
FT /evidence="ECO:0007829|PDB:1HUU"
SQ SEQUENCE 90 AA; 9716 MW; 4F51530D032C071E CRC64;
MNKTELINAV AETSGLSKKD ATKAVDAVFD SITEALRKGD KVQLIGFGNF EVRERAARKG
RNPQTGEEME IPASKVPAFK PGKALKDAVK