ID   DN7B_SACSH              Reviewed;          64 AA.
AC   O59632;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=DNA-binding protein 7b {ECO:0000305};
DE   AltName: Full=7 kDa DNA-binding protein B;
DE   AltName: Full=Ssh7b {ECO:0000303|PubMed:27853299};
GN   Name=ssh7b {ECO:0000312|EMBL:BAA28275.1};
OS   Saccharolobus shibatae (Sulfolobus shibatae).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=2286;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-12, FUNCTION,
RP   METHYLATION AT LYS-5 AND LYS-7, AND DNA-BINDING.
RC   STRAIN=ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12;
RX   PubMed=9573212; DOI=10.1128/jb.180.9.2560-2563.1998;
RA   Mai V.Q., Chen X., Hong R., Huang L.;
RT   "Small abundant DNA binding proteins from the thermoacidophilic archaeon
RT   Sulfolobus shibatae constrain negative DNA supercoils.";
RL   J. Bacteriol. 180:2560-2563(1998).
RN   [2]
RP   DNA-BINDING, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, SUBCELLULAR LOCATION,
RP   AND NOMENCLATURE.
RX   PubMed=27853299; DOI=10.1038/srep37274;
RA   Kalichuk V., Behar G., Renodon-Corniere A., Danovski G., Obal G.,
RA   Barbet J., Mouratou B., Pecorari F.;
RT   "The archaeal '7 kDa DNA-binding' proteins: extended characterization of an
RT   old gifted family.";
RL   Sci. Rep. 6:37274-37274(2016).
CC   -!- FUNCTION: Can constrain negative DNA supercoils (PubMed:9573212). May
CC       be involved in maintaining the integrity of the genome at high
CC       temperature (Probable). {ECO:0000269|PubMed:9573212,
CC       ECO:0000305|PubMed:9573212}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Highly stable from pH 0 to pH 12. {ECO:0000269|PubMed:27853299};
CC       Temperature dependence:
CC         Hyperthermostable. {ECO:0000269|PubMed:27853299};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:27853299}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27853299}.
CC   -!- PTM: Lys-5 and Lys-7 may be methylated. {ECO:0000305|PubMed:9573212}.
CC   -!- SIMILARITY: Belongs to the 7 kDa DNA-binding/endoribonuclease P2
CC       family. {ECO:0000305}.
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DR   EMBL; AB013923; BAA28275.1; -; Genomic_DNA.
DR   RefSeq; WP_012712662.1; NZ_CP077715.1.
DR   AlphaFoldDB; O59632; -.
DR   SMR; O59632; -.
DR   iPTMnet; O59632; -.
DR   GeneID; 7941807; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro.
DR   InterPro; IPR016197; Chromo-like_dom_sf.
DR   InterPro; IPR003212; DNA-bd_7kDa_arc.
DR   Pfam; PF02294; 7kD_DNA_binding; 1.
DR   PIRSF; PIRSF036912; Sac7; 1.
DR   SUPFAM; SSF54160; SSF54160; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; DNA-binding; Methylation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:9573212"
FT   CHAIN           2..64
FT                   /note="DNA-binding protein 7b"
FT                   /id="PRO_0000213079"
FT   MOD_RES         5
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000305|PubMed:9573212"
FT   MOD_RES         7
FT                   /note="N6-methyllysine"
FT                   /evidence="ECO:0000305|PubMed:9573212"
SQ   SEQUENCE   64 AA;  7296 MW;  D88FCC7027B953D1 CRC64;
     MVTVKFKYKG EEKEVDTSKI KKVWRVGKMI SFTYDEGGGK TGRGAVSEKD APKELLQMLE
     KQKK