SSB_SACS2
ID SSB_SACS2 Reviewed; 148 AA.
AC Q97W73;
DT 11-JUN-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 25-MAY-2022, entry version 109.
DE RecName: Full=Single-stranded DNA binding protein Ssb;
DE Short=SSB;
GN Name=ssb; OrderedLocusNames=SSO2364;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=12675797; DOI=10.1046/j.1365-2958.2003.03444.x;
RA Roberts J.A., Bell S.D., White M.F.;
RT "An archaeal XPF repair endonuclease dependent on a heterotrimeric PCNA.";
RL Mol. Microbiol. 48:361-371(2003).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.20 ANGSTROMS) OF 1-119, SUBUNIT, DNA-BINDING, AND
RP MUTAGENESIS OF ILE-30; TRP-56; TRP-75 AND PHE-79.
RX PubMed=12773373; DOI=10.1093/emboj/cdg272;
RA Kerr I.D., Wadsworth R.I., Cubeddu L., Blankenfeldt W., Naismith J.H.,
RA White M.F.;
RT "Insights into ssDNA recognition by the OB fold from a structural and
RT thermodynamic study of Sulfolobus SSB protein.";
RL EMBO J. 22:2561-2570(2003).
CC -!- FUNCTION: Binds to ssDNA, binding approximately 5 nucleotides per
CC monomer. Binding my be slightly cooperative. Inhibits the endonuclease
CC activity of XPF. {ECO:0000269|PubMed:12675797}.
CC -!- SUBUNIT: Monomer in solution, may bind ssDNA as an array of monomers.
CC {ECO:0000305|PubMed:12773373}.
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DR EMBL; AE006641; AAK42515.1; -; Genomic_DNA.
DR PIR; D90407; D90407.
DR RefSeq; WP_009989484.1; NC_002754.1.
DR PDB; 1O7I; X-ray; 1.20 A; A/B=1-119.
DR PDB; 2MNA; NMR; -; A=1-114.
DR PDBsum; 1O7I; -.
DR PDBsum; 2MNA; -.
DR AlphaFoldDB; Q97W73; -.
DR BMRB; Q97W73; -.
DR SMR; Q97W73; -.
DR STRING; 273057.SSO2364; -.
DR EnsemblBacteria; AAK42515; AAK42515; SSO2364.
DR GeneID; 44128089; -.
DR KEGG; sso:SSO2364; -.
DR PATRIC; fig|273057.12.peg.2449; -.
DR eggNOG; arCOG01510; Archaea.
DR HOGENOM; CLU_110881_2_0_2; -.
DR InParanoid; Q97W73; -.
DR OMA; AWTTSYR; -.
DR PhylomeDB; Q97W73; -.
DR EvolutionaryTrace; Q97W73; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IBA:GO_Central.
DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central.
DR Gene3D; 2.40.50.140; -; 1.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Reference proteome.
FT CHAIN 1..148
FT /note="Single-stranded DNA binding protein Ssb"
FT /id="PRO_0000429325"
FT DNA_BIND 19..88
FT /note="OB"
FT REGION 90..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..117
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 30
FT /note="I->A: Slight decrease in ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12773373"
FT MUTAGEN 56
FT /note="W->A: Significantly weaker ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12773373"
FT MUTAGEN 75
FT /note="W->A: Slight decrease in ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12773373"
FT MUTAGEN 79
FT /note="F->A: Significantly weaker ssDNA binding."
FT /evidence="ECO:0000269|PubMed:12773373"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 13..24
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 28..30
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 37..46
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 49..56
FT /evidence="ECO:0007829|PDB:1O7I"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1O7I"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:2MNA"
FT STRAND 68..79
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 82..87
FT /evidence="ECO:0007829|PDB:1O7I"
FT STRAND 92..95
FT /evidence="ECO:0007829|PDB:1O7I"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1O7I"
SQ SEQUENCE 148 AA; 16138 MW; 84147186545E763D CRC64;
MEEKVGNLKP NMESVNVTVR VLEASEARQI QTKNGVRTIS EAIVGDETGR VKLTLWGKHA
GSIKEGQVVK IENAWTTAFK GQVQLNAGSK TKIAEASEDG FPESSQIPEN TPTAPQQMRG
GGRGFRGGGR RYGRRGGRRQ ENEEGEEE
