DBH2_STRCO
ID DBH2_STRCO Reviewed; 218 AA.
AC P0A3H7; O86537;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=DNA-binding protein HU 2;
GN Name=hup2; OrderedLocusNames=SCO5556; ORFNames=SC1C2.37;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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. {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC {ECO:0000305}.
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DR EMBL; AL939124; CAA20004.1; -; Genomic_DNA.
DR PIR; T29086; T29086.
DR RefSeq; NP_629690.1; NC_003888.3.
DR RefSeq; WP_003973439.1; NZ_VNID01000011.1.
DR AlphaFoldDB; P0A3H7; -.
DR SMR; P0A3H7; -.
DR STRING; 100226.SCO5556; -.
DR GeneID; 1100996; -.
DR KEGG; sco:SCO5556; -.
DR PATRIC; fig|100226.15.peg.5644; -.
DR eggNOG; COG0776; Bacteria.
DR HOGENOM; CLU_085366_0_0_11; -.
DR InParanoid; P0A3H7; -.
DR OMA; AQFKAVI; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA condensation; DNA-binding; Reference proteome.
FT CHAIN 1..218
FT /note="DNA-binding protein HU 2"
FT /id="PRO_0000104975"
FT REGION 1..91
FT /note="Bacterial histone-like domain"
FT REGION 101..218
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 118..218
FT /note="Degenerate repeats region"
FT COMPBIAS 149..178
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..218
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 218 AA; 22348 MW; E66F7809B5016AA7 CRC64;
MNKAQLVEAI ADKLGGRQQA ADAVDAVLDA LVRAVVAGDR VSVTGFGSFE KVDRPARYAR
NPQTGERVRV KKTSVPRFRA GQGFKDLVSG SKKLPKNDIA VKKAPKGSLS GPPPTISKAA
GKKAAAKKAT GAAKKTTGAA KKTSAAAKKT TAKKTTGAAK TTAKKTTAKK SAAKTTTAAA
KKTAAKKAPA KKATAKKAPA KKSTARKTTA KKATARKK