HMT2_METTH
ID HMT2_METTH Reviewed; 68 AA.
AC O27731;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=DNA-binding protein HMt-1.2;
DE AltName: Full=Archaeal histone A2;
GN Name=hmtA2; OrderedLocusNames=MTH_1696;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
CC -!- FUNCTION: Binds and compacts DNA (95 to 150 base pairs) to form
CC nucleosome-like structures that contain positive DNA supercoils.
CC {ECO:0000250|UniProtKB:P50483}.
CC -!- SUBUNIT: Homodimer or heterodimer with HmtB (By similarity). Dimers
CC then assemble into higher oligomers, with the DNA wrapped around the
CC protein core (By similarity). {ECO:0000250|UniProtKB:P19267,
CC ECO:0000250|UniProtKB:P50483}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P50483}.
CC Chromosome {ECO:0000250|UniProtKB:P50483}.
CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR EMBL; AE000666; AAB86168.1; -; Genomic_DNA.
DR PIR; G69093; G69093.
DR RefSeq; WP_010877303.1; NC_000916.1.
DR AlphaFoldDB; O27731; -.
DR SMR; O27731; -.
DR STRING; 187420.MTH_1696; -.
DR PRIDE; O27731; -.
DR EnsemblBacteria; AAB86168; AAB86168; MTH_1696.
DR GeneID; 1470781; -.
DR KEGG; mth:MTH_1696; -.
DR PATRIC; fig|187420.15.peg.1656; -.
DR HOGENOM; CLU_192667_0_0_2; -.
DR OMA; CKHAGRK; -.
DR Proteomes; UP000005223; 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:0006352; P:DNA-templated transcription, initiation; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR003958; CBFA_NFYB_domain.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR004823; TAF_TATA-bd_Histone-like_dom.
DR Pfam; PF00808; CBFD_NFYB_HMF; 1.
DR SMART; SM00803; TAF; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 3: Inferred from homology;
KW Chromosome; Cytoplasm; DNA-binding; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..68
FT /note="DNA-binding protein HMt-1.2"
FT /id="PRO_0000154992"
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 SITE 14
FT /note="Interaction with DNA"
FT /evidence="ECO:0000250|UniProtKB:P19267"
SQ SEQUENCE 68 AA; 7275 MW; 70530AED87AB7206 CRC64;
MAELPIAPVG RIIKNAGAQR ISDDAREALA KILEEKGEEI AKEAVKLAKH AGRKTVKASD
IELAAKKL
