ID   Y729_METJA              Reviewed;         124 AA.
AC   Q58139;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=CBS domain-containing protein MJ0729 {ECO:0000305};
GN   OrderedLocusNames=MJ0729;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   CRYSTALLIZATION, AND SUBUNIT.
RX   PubMed=18607087; DOI=10.1107/s1744309108013432;
RA   Fernandez-Millan P., Kortazar D., Lucas M., Martinez-Chantar M.L.,
RA   Astigarraga E., Fernandez J.A., Sabas O., Albert A., Mato J.M.,
RA   Martinez-Cruz L.A.;
RT   "Crystallization and preliminary crystallographic analysis of merohedrally
RT   twinned crystals of MJ0729, a CBS-domain protein from Methanococcus
RT   jannaschii.";
RL   Acta Crystallogr. F 64:605-609(2008).
RN   [3]
RP   SUBUNIT.
RX   PubMed=19267448; DOI=10.1021/bi801920r;
RA   Martinez-Cruz L.A., Encinar J.A., Kortazar D., Prieto J., Gomez J.,
RA   Fernandez-Millan P., Lucas M., Arribas E.A., Fernandez J.A.,
RA   Martinez-Chantar M.L., Mato J.M., Neira J.L.;
RT   "The CBS domain protein MJ0729 of Methanocaldococcus jannaschii is a
RT   thermostable protein with a pH-dependent self-oligomerization.";
RL   Biochemistry 48:2760-2776(2009).
RN   [4]
RP   DNA-BINDING, AND DOMAIN.
RX   PubMed=20934423; DOI=10.1016/j.febslet.2010.10.006;
RA   Aguado-Llera D., Oyenarte I., Martinez-Cruz L.A., Neira J.L.;
RT   "The CBS domain protein MJ0729 of Methanocaldococcus jannaschii binds
RT   DNA.";
RL   FEBS Lett. 584:4485-4489(2010).
RN   [5]
RP   DOMAIN.
RX   PubMed=20959390; DOI=10.1093/protein/gzq073;
RA   Martinez-Cruz L.A., Encinar J.A., Sevilla P., Oyenarte I., Gomez-Garcia I.,
RA   Aguado-Llera D., Garcia-Blanco F., Gomez J., Neira J.L.;
RT   "Nucleotide-induced conformational transitions in the CBS domain protein
RT   MJ0729 of Methanocaldococcus jannaschii.";
RL   Protein Eng. Des. Sel. 24:161-169(2011).
CC   -!- SUBUNIT: Exhibits a pH-dependent oligomerization state: at pH 7, the
CC       dominant species is a dimer, where each monomer is a two-CBS domain
CC       protein, and at pH 4.5-4.8, the dominant species is a tetramer, with an
CC       oblong shape (PubMed:18607087, PubMed:19267448). At pH 2.5, there is
CC       formation of intermolecular hydrogen bonds, suggesting the presence of
CC       high-molecular weight species (PubMed:19267448). The physiological
CC       dimeric species is thermal and chemically very stable
CC       (PubMed:19267448). {ECO:0000269|PubMed:18607087,
CC       ECO:0000269|PubMed:19267448}.
CC   -!- DOMAIN: The CBS domains bind adenosine derivatives (AMP, ATP, NADP and
CC       SAM) (PubMed:20959390). The CBS domains can also bind calf-thymus DNA
CC       and E-boxes recognized by transcription factors (PubMed:20934423).
CC       Binding of the nucleotides induces protein conformational changes
CC       (PubMed:20934423, PubMed:20959390). {ECO:0000269|PubMed:20934423,
CC       ECO:0000269|PubMed:20959390}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; L77117; AAB98725.1; -; Genomic_DNA.
DR   PIR; A64391; A64391.
DR   AlphaFoldDB; Q58139; -.
DR   SMR; Q58139; -.
DR   STRING; 243232.MJ_0729; -.
DR   EnsemblBacteria; AAB98725; AAB98725; MJ_0729.
DR   KEGG; mja:MJ_0729; -.
DR   eggNOG; arCOG00629; Archaea.
DR   HOGENOM; CLU_2044437_0_0_2; -.
DR   OMA; CKHSKIE; -.
DR   PhylomeDB; Q58139; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.580.10; -; 2.
DR   InterPro; IPR000644; CBS_dom.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   Pfam; PF00571; CBS; 2.
DR   SMART; SM00116; CBS; 2.
DR   SUPFAM; SSF54631; SSF54631; 1.
DR   PROSITE; PS51371; CBS; 2.
PE   1: Evidence at protein level;
KW   CBS domain; DNA-binding; Reference proteome; Repeat.
FT   CHAIN           1..124
FT                   /note="CBS domain-containing protein MJ0729"
FT                   /id="PRO_0000107005"
FT   DOMAIN          10..67
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          70..124
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
SQ   SEQUENCE   124 AA;  14303 MW;  1C0AAF097936B34A CRC64;
     MMIMKVKEVM NKDFIKISPN DIGGEVVQTL YKEKKNYAPV IEDGKLVGWI TALDLLIGCK
     HSKIEDLMLL IDEIKILKEN DEVTDELIDE IIKNEDIAYP VINDRDEVVG TLSVFDLLKY
     YKNR