ID   HMFA_METFE              Reviewed;          69 AA.
AC   P48781;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=DNA-binding protein HMf-1 {ECO:0000303|PubMed:2377617};
DE   AltName: Full=Archaeal histone A;
GN   Name=hmfA {ECO:0000303|PubMed:7809089};
OS   Methanothermus fervidus.
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanothermaceae; Methanothermus.
OX   NCBI_TaxID=2180;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-67.
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   PROTEIN SEQUENCE OF 1-35, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=2377617; DOI=10.1073/pnas.87.15.5788;
RA   Sandman K.M., Krzycki J.A., Dobrinski B., Lurz R., Reeve J.N.;
RT   "HMf, a DNA-binding protein isolated from the hyperthermophilic archaeon
RT   Methanothermus fervidus, is most closely related to histones.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5788-5791(1990).
RN   [3]
RP   FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND INDUCTION.
RX   PubMed=7809089; DOI=10.1073/pnas.91.26.12624;
RA   Sandman K.M., Grayling R.A., Dobrinski B., Lurz R., Reeve J.N.;
RT   "Growth-phase-dependent synthesis of histones in the archaeon
RT   Methanothermus fervidus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:12624-12628(1994).
RN   [4]
RP   CRYSTALLIZATION.
RX   PubMed=8820495;
RX   DOI=10.1002/(sici)1097-0134(199602)24:2<269::aid-prot16>3.0.co;2-l;
RA   Decanniere K., Sandman K., Reeve J.N., Heinemann U.;
RT   "Crystallization and preliminary X-ray characterization of the
RT   Methanothermus fervidus histones HMfA and HMfB.";
RL   Proteins 24:269-271(1996).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS), AND SUBUNIT.
RX   PubMed=11021968; DOI=10.1006/jmbi.2000.4104;
RA   Decanniere K., Babu A.M., Sandman K., Reeve J.N., Heinemann U.;
RT   "Crystal structures of recombinant histones HMfA and HMfB from the
RT   hyperthermophilic archaeon Methanothermus fervidus.";
RL   J. Mol. Biol. 303:35-47(2000).
CC   -!- FUNCTION: Binds and compacts DNA (95 to 150 base pairs) to form
CC       nucleosome-like structures that contain positive DNA supercoils.
CC       Increases the resistance of DNA to thermal denaturation.
CC       {ECO:0000269|PubMed:2377617, ECO:0000269|PubMed:7809089}.
CC   -!- SUBUNIT: Homodimer and heterodimer of HmfA and HmfB (PubMed:2377617,
CC       PubMed:7809089, PubMed:11021968). Forms primarily homodimers during
CC       exponential phase, and heterodimers appear when cells enter stationary
CC       phase (PubMed:7809089). Dimers then assemble into higher oligomers,
CC       with the DNA wrapped around the protein core (By similarity).
CC       {ECO:0000250|UniProtKB:P19267, ECO:0000269|PubMed:11021968,
CC       ECO:0000269|PubMed:2377617, ECO:0000269|PubMed:7809089}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2377617}.
CC       Chromosome {ECO:0000305|PubMed:2377617, ECO:0000305|PubMed:7809089}.
CC   -!- INDUCTION: Expressed at constant, high levels during exponential growth
CC       and during stationary phase. {ECO:0000269|PubMed:7809089}.
CC   -!- SIMILARITY: Belongs to the archaeal histone HMF family. {ECO:0000305}.
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DR   EMBL; M96826; AAA73366.1; -; Genomic_DNA.
DR   PIR; A47036; A47036.
DR   PIR; T48848; T48848.
DR   RefSeq; WP_013413995.1; NC_014658.1.
DR   PDB; 1B67; X-ray; 1.48 A; A/B=2-69.
DR   PDB; 1HTA; X-ray; 1.55 A; A=1-69.
DR   PDBsum; 1B67; -.
DR   PDBsum; 1HTA; -.
DR   AlphaFoldDB; P48781; -.
DR   SMR; P48781; -.
DR   GeneID; 9962656; -.
DR   OMA; MANDLPI; -.
DR   EvolutionaryTrace; P48781; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR   GO; GO:0046982; F:protein heterodimerization activity; IDA:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR   GO; GO:0006265; P:DNA topological change; IDA:UniProtKB.
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   3D-structure; Chromosome; Cytoplasm; Direct protein sequencing;
KW   DNA-binding.
FT   CHAIN           1..69
FT                   /note="DNA-binding protein HMf-1"
FT                   /id="PRO_0000154982"
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"
FT   HELIX           6..15
FT                   /evidence="ECO:0007829|PDB:1B67"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:1B67"
FT   HELIX           23..50
FT                   /evidence="ECO:0007829|PDB:1B67"
FT   STRAND          54..56
FT                   /evidence="ECO:0007829|PDB:1B67"
FT   HELIX           58..64
FT                   /evidence="ECO:0007829|PDB:1B67"
FT   HELIX           65..68
FT                   /evidence="ECO:0007829|PDB:1B67"
SQ   SEQUENCE   69 AA;  7500 MW;  4E10263F58F175F3 CRC64;
     MGELPIAPIG RIIKNAGAER VSDDARIALA KVLEEMGEEI ASEAVKLAKH AGRKTIKAED
     IELARKMFK