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Database: UniProt
Entry: A0LVA1_ACIC1
LinkDB: A0LVA1_ACIC1
Original site: A0LVA1_ACIC1 
ID   A0LVA1_ACIC1            Unreviewed;       163 AA.
AC   A0LVA1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   SubName: Full=Histone family protein DNA-binding protein {ECO:0000313|EMBL:ABK53361.1};
GN   OrderedLocusNames=Acel_1589 {ECO:0000313|EMBL:ABK53361.1};
OS   Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC   Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC   Acidothermus.
OX   NCBI_TaxID=351607 {ECO:0000313|EMBL:ABK53361.1, ECO:0000313|Proteomes:UP000008221};
RN   [1] {ECO:0000313|EMBL:ABK53361.1, ECO:0000313|Proteomes:UP000008221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43068 / DSM 8971 / 11B
RC   {ECO:0000313|Proteomes:UP000008221};
RX   PubMed=19270083; DOI=10.1101/gr.084848.108;
RA   Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA   Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA   Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT   "Complete genome of the cellulolytic thermophile Acidothermus
RT   cellulolyticus 11B provides insights into its ecophysiological and
RT   evolutionary adaptations.";
RL   Genome Res. 19:1033-1043(2009).
CC   -!- SIMILARITY: Belongs to the bacterial histone-like protein family.
CC       {ECO:0000256|RuleBase:RU003939}.
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DR   EMBL; CP000481; ABK53361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0LVA1; -.
DR   STRING; 351607.Acel_1589; -.
DR   KEGG; ace:Acel_1589; -.
DR   eggNOG; COG0776; Bacteria.
DR   HOGENOM; CLU_085366_1_0_11; -.
DR   InParanoid; A0LVA1; -.
DR   OrthoDB; 9799835at2; -.
DR   Proteomes; UP000008221; Chromosome.
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   CDD; cd13831; HU; 1.
DR   Gene3D; 4.10.520.10; IHF-like DNA-binding proteins; 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; DNA-BINDING PROTEIN HU; 1.
DR   PANTHER; PTHR33175:SF3; DNA-BINDING PROTEIN HU-BETA; 1.
DR   Pfam; PF00216; Bac_DNA_binding; 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   DNA condensation {ECO:0000256|ARBA:ARBA00023067};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000313|EMBL:ABK53361.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008221}.
FT   REGION          114..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        142..163
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   163 AA;  16851 MW;  0D3D4D58C0278FAE CRC64;
     MNKAELITAV AARIGDKKTA SEAVEAVIDT ITRTVARGEK VAITGFGIFE KVERAARMAR
     NPATGERVRV KKTSVPKFRA GTRLKGVVSG AIKLPAVKAA PAAKPAKAAK AAKAAPAKAA
     GRRGAAKAAG RAAARATRKV TATRRTATKK TAARRTTGRR GGR
//
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