DN7A_SACSH
ID DN7A_SACSH Reviewed; 64 AA.
AC P61990; O59631; P80170; Q9UWI8;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 55.
DE RecName: Full=DNA-binding protein 7a {ECO:0000305};
DE AltName: Full=7 kDa DNA-binding protein a;
DE AltName: Full=Ssh7a {ECO:0000303|PubMed:27853299};
GN Name=ssh7a {ECO:0000312|EMBL:BAA28274.1};
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 DNA-BINDING, AND METHYLATION AT LYS-5 AND LYS-7.
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:0000250|UniProtKB:P61991,
CC 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; AB013922; BAA28274.1; -; Genomic_DNA.
DR RefSeq; WP_009992021.1; NZ_CP077715.1.
DR AlphaFoldDB; P61990; -.
DR BMRB; P61990; -.
DR SMR; P61990; -.
DR iPTMnet; P61990; -.
DR GeneID; 7812726; -.
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; Hydrolase; Methylation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9573212"
FT CHAIN 2..64
FT /note="DNA-binding protein 7a"
FT /id="PRO_0000213076"
FT MOD_RES 5
FT /note="N6-methylated lysine; partial"
FT /evidence="ECO:0000250|UniProtKB:P61991,
FT ECO:0000305|PubMed:9573212"
FT MOD_RES 7
FT /note="N6-methylated lysine; partial"
FT /evidence="ECO:0000250|UniProtKB:P61991,
FT ECO:0000305|PubMed:9573212"
SQ SEQUENCE 64 AA; 7279 MW; 0E4BA126FCCF84DD CRC64;
MATVKFKYKG EEKQVDISKI KKVWRVGKMI SFTYDEGGGK TGRGAVSEKD APKELLQMLE
KQKK
