ID C1B2N2_RHOOB Unreviewed; 231 AA.
AC C1B2N2;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 98.
DE RecName: Full=DNA-binding protein HupB {ECO:0000256|ARBA:ARBA00035692};
DE EC=1.16.3.1 {ECO:0000256|ARBA:ARBA00013107};
DE AltName: Full=Histone-like protein {ECO:0000256|ARBA:ARBA00032423};
GN Name=hup {ECO:0000313|EMBL:BAH54799.1};
GN OrderedLocusNames=ROP_65520 {ECO:0000313|EMBL:BAH54799.1};
OS Rhodococcus opacus (strain B4).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=632772 {ECO:0000313|EMBL:BAH54799.1, ECO:0000313|Proteomes:UP000002212};
RN [1] {ECO:0000313|EMBL:BAH54799.1, ECO:0000313|Proteomes:UP000002212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B4 {ECO:0000313|EMBL:BAH54799.1,
RC ECO:0000313|Proteomes:UP000002212};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Might have a role in establishing the nucleoid structure of
CC elementary bodies. {ECO:0000256|ARBA:ARBA00002344}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC Evidence={ECO:0000256|ARBA:ARBA00035572};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11149;
CC Evidence={ECO:0000256|ARBA:ARBA00035572};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, nucleoid
CC {ECO:0000256|ARBA:ARBA00004453}.
CC -!- SIMILARITY: Belongs to the bacterial histone-like protein family. Long
CC actinobacterial subfamily. {ECO:0000256|ARBA:ARBA00035660}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. HCT subfamily.
CC {ECO:0000256|ARBA:ARBA00008424}.
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DR EMBL; AP011115; BAH54799.1; -; Genomic_DNA.
DR RefSeq; WP_015890245.1; NC_012522.1.
DR AlphaFoldDB; C1B2N2; -.
DR STRING; 632772.ROP_65520; -.
DR KEGG; rop:ROP_65520; -.
DR PATRIC; fig|632772.20.peg.6838; -.
DR HOGENOM; CLU_085366_0_0_11; -.
DR OMA; VPTFRPG; -.
DR OrthoDB; 9799835at2; -.
DR Proteomes; UP000002212; Chromosome.
DR GO; GO:0009295; C:nucleoid; IEA:UniProtKB-SubCell.
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:InterPro.
DR CDD; cd13831; HU; 1.
DR Gene3D; 4.10.520.10; IHF-like DNA-binding proteins; 1.
DR InterPro; IPR009970; HC2.
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; DNA-BINDING PROTEIN HU; 1.
DR PANTHER; PTHR33175:SF3; DNA-BINDING PROTEIN HU-BETA; 1.
DR Pfam; PF00216; Bac_DNA_binding; 1.
DR Pfam; PF07382; HC2; 1.
DR PRINTS; PR01727; DNABINDINGHU.
DR SMART; SM00411; BHL; 1.
DR SUPFAM; SSF47729; IHF-like DNA-binding proteins; 1.
DR PROSITE; PS00045; HISTONE_LIKE; 1.
PE 3: Inferred from homology;
KW Acetylation {ECO:0000256|ARBA:ARBA00022990};
KW DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:BAH54799.1}.
FT REGION 147..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 231 AA; 23497 MW; 98ED87641C635293 CRC64;
MNKAELIDVL TEKLGTDRRT ATEAVEHVVD TIVRAVHRGD SVTITGFGVF EQRRRAARVA
RNPRTGETVK VKPTSVPAFR PGAQFKAVIA GGQKLPATGP AVKRGAAAPA TKAAAKKAAA
KKTAAKKTAA KKAPAKTAAA KKTVAKKVAP AKTAAAKKTV AKKVAPAKTA AAKKTAAKKA
PAKTAAAKKT VAKKVAPAKT AAAKKTAAKK APAKTAAKKT AAKKAPAKRA K
//