DBH_BACCL
ID DBH_BACCL Reviewed; 90 AA.
AC P0A3H1; P02346; P08822;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 53.
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 Bacillus caldolyticus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=1394;
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 PROTEIN SEQUENCE OF 1-39.
RX PubMed=3566914; DOI=10.1515/bchm3.1987.368.1.121;
RA Beck A., Dijk J., Reinhardt R.;
RT "Ribosomal proteins and DNA-binding protein II from the extreme thermophile
RT Bacillus caldolyticus.";
RL Biol. Chem. Hoppe-Seyler 368:121-130(1987).
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; M73502; AAA22534.1; -; Genomic_DNA.
DR PIR; JC1207; JC1207.
DR AlphaFoldDB; P0A3H1; -.
DR BMRB; P0A3H1; -.
DR SMR; P0A3H1; -.
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 Direct protein sequencing; DNA condensation; DNA-binding; Phosphoprotein.
FT CHAIN 1..90
FT /note="DNA-binding protein HU"
FT /id="PRO_0000104909"
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 CONFLICT 9
FT /note="A -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="T -> I (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 30
FT /note="D -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 90 AA; 9716 MW; 4F51530D032C071E CRC64;
MNKTELINAV AETSGLSKKD ATKAVDAVFD SITEALRKGD KVQLIGFGNF EVRERAARKG
RNPQTGEEME IPASKVPAFK PGKALKDAVK