ID   HMTB_METTH              Reviewed;          67 AA.
AC   P50484;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=DNA-binding protein HMt-2 {ECO:0000303|PubMed:1459937};
DE   AltName: Full=Archaeal histone A;
GN   Name=hmtB {ECO:0000303|PubMed:1459937}; OrderedLocusNames=MTH_254;
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 [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION, AND
RP   SUBUNIT.
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=1459937; DOI=10.1128/jb.174.24.7890-7895.1992;
RA   Tabassum R., Sandman K.M., Reeve J.N.;
RT   "HMt, a histone-related protein from Methanobacterium thermoautotrophicum
RT   delta H.";
RL   J. Bacteriol. 174:7890-7895(1992).
RN   [2]
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 compact DNA (95 to 150 base pairs) to form
CC       nucleosome-like structures that contain positive DNA supercoils.
CC       {ECO:0000269|PubMed:1459937}.
CC   -!- SUBUNIT: Homodimer or heterodimer with HmtA1 or HmtA2 (PubMed:1459937).
CC       Dimers then assemble into higher oligomers, with the DNA wrapped around
CC       the protein core (By similarity). {ECO:0000250|UniProtKB:P19267,
CC       ECO:0000269|PubMed:1459937}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1459937}.
CC       Chromosome {ECO:0000305|PubMed:1459937}.
CC   -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB84760.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M86663; AAA73196.1; -; Genomic_DNA.
DR   EMBL; AE000666; AAB84760.1; ALT_INIT; Genomic_DNA.
DR   PIR; C47036; C47036.
DR   RefSeq; WP_048060781.1; NC_000916.1.
DR   AlphaFoldDB; P50484; -.
DR   SMR; P50484; -.
DR   STRING; 187420.MTH_254; -.
DR   EnsemblBacteria; AAB84760; AAB84760; MTH_254.
DR   GeneID; 1470215; -.
DR   KEGG; mth:MTH_254; -.
DR   PATRIC; fig|187420.15.peg.223; -.
DR   HOGENOM; CLU_192667_0_0_2; -.
DR   OMA; VEWANHA; -.
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   1: Evidence at protein level;
KW   Chromosome; Cytoplasm; DNA-binding; Reference proteome.
FT   CHAIN           1..67
FT                   /note="DNA-binding protein HMt-2"
FT                   /id="PRO_0000154993"
FT   REGION          53..56
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
FT   SITE            13
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250|UniProtKB:P19267"
SQ   SEQUENCE   67 AA;  7149 MW;  C39FF4EA05287B46 CRC64;
     MELPIAPIGR IIKNAGAEIV SDDAREALAK VLEAKGEEIA ENAVKLAKHA GRKTVKASDI
     ELAVKRM