HARA_THEKO
ID HARA_THEKO Reviewed; 67 AA.
AC Q9Y8I1;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Archaeal histone A;
DE AltName: Full=Archaeal histone A1;
GN Name=hpkA; OrderedLocusNames=TK1413;
OS Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS (Pyrococcus kodakaraensis (strain KOD1)).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=69014;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=10329402; DOI=10.1006/bbrc.1999.0533;
RA Higashibata H., Fujiwara S., Takagi M., Imanaka T.;
RT "Analysis of DNA compaction profile and intracellular contents of archaeal
RT histones from Pyrococcus kodakaraensis KOD1.";
RL Biochem. Biophys. Res. Commun. 258:416-424(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=15710748; DOI=10.1101/gr.3003105;
RA Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL Genome Res. 15:352-363(2005).
RN [3]
RP FUNCTION, SUBCELLULAR LOCATION, AND DNA-BINDING.
RC STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX PubMed=21148291; DOI=10.1091/mbc.e10-08-0668;
RA Maruyama H., Shin M., Oda T., Matsumi R., Ohniwa R.L., Itoh T.,
RA Shirahige K., Imanaka T., Atomi H., Yoshimura S.H., Takeyasu K.;
RT "Histone and TK0471/TrmBL2 form a novel heterogeneous genome architecture
RT in the hyperthermophilic archaeon Thermococcus kodakarensis.";
RL Mol. Biol. Cell 22:386-398(2011).
RN [4]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF GLY-17.
RX PubMed=28798133; DOI=10.1126/science.aaj1849;
RA Mattiroli F., Bhattacharyya S., Dyer P.N., White A.E., Sandman K.,
RA Burkhart B.W., Byrne K.R., Lee T., Ahn N.G., Santangelo T.J., Reeve J.N.,
RA Luger K.;
RT "Structure of histone-based chromatin in Archaea.";
RL Science 357:609-612(2017).
CC -!- FUNCTION: Binds and compacts DNA (about 120 base pairs per nucleosome,
CC corresponding to four histone dimers) to form nucleosome-like
CC structures. {ECO:0000269|PubMed:10329402, ECO:0000269|PubMed:21148291,
CC ECO:0000269|PubMed:28798133}.
CC -!- SUBUNIT: Homodimer or heterodimer. Dimers then assemble into higher
CC oligomers, with the DNA wrapped around the protein core. Higher order
CC oligomerization of these structures can give rise to long, superhelical
CC fibers (in vitro). {ECO:0000305|PubMed:28798133}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21148291}.
CC Chromosome {ECO:0000269|PubMed:21148291}.
CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR EMBL; AB016003; BAA77575.1; -; Genomic_DNA.
DR EMBL; AP006878; BAD85602.1; -; Genomic_DNA.
DR RefSeq; WP_011250364.1; NC_006624.1.
DR AlphaFoldDB; Q9Y8I1; -.
DR SMR; Q9Y8I1; -.
DR STRING; 69014.TK1413; -.
DR PRIDE; Q9Y8I1; -.
DR EnsemblBacteria; BAD85602; BAD85602; TK1413.
DR GeneID; 3234267; -.
DR KEGG; tko:TK1413; -.
DR PATRIC; fig|69014.16.peg.1375; -.
DR eggNOG; arCOG02144; Archaea.
DR HOGENOM; CLU_192667_0_0_2; -.
DR InParanoid; Q9Y8I1; -.
DR OMA; CKHAGRK; -.
DR PhylomeDB; Q9Y8I1; -.
DR Proteomes; UP000000536; Chromosome.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA condensation; DNA-binding; Reference proteome.
FT CHAIN 1..67
FT /note="Archaeal histone A"
FT /id="PRO_0000154997"
FT REGION 20..22
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P19267"
FT REGION 54..57
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P19267"
FT MUTAGEN 17
FT /note="G->D,L,S: Expected to impair oligomerization. Alters
FT compaction of DNA on nucleosome-like structures. Delays
FT adaptation to a sulfur-free medium due to impaired
FT transcriptional activation of genes required for growth on
FT a sulfur-free medium."
FT /evidence="ECO:0000269|PubMed:28798133"
SQ SEQUENCE 67 AA; 7379 MW; C8C608B526D0A618 CRC64;
MAELPIAPVD RLIRKAGAER VSEDAAKVLA EYLEEYAIEL SKKAVDFARH AGRKTVKAED
IKLAIKA
