SSB_THEAQ
ID SSB_THEAQ Reviewed; 264 AA.
AC Q9KH06;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 85.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_00984};
DE Short=SSB {ECO:0000255|HAMAP-Rule:MF_00984};
GN Name=ssb;
OS Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT.
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=12368464; DOI=10.1099/00221287-148-10-3307;
RA Dabrowski S., Olszewski M., Piatek R., Brillowska-Dabrowska A., Konopa G.,
RA Kur J.;
RT "Identification and characterization of single-stranded-DNA-binding
RT proteins from Thermus thermophilus and Thermus aquaticus -- new arrangement
RT of binding domains.";
RL Microbiology 148:3307-3315(2002).
CC -!- FUNCTION: Plays an important role in DNA replication, recombination and
CC repair. Binds to ssDNA and to an array of partner proteins to recruit
CC them to their sites of action during DNA metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_00984}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12368464}.
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DR EMBL; AF276705; AAF85976.1; -; Genomic_DNA.
DR RefSeq; WP_053767427.1; NZ_LHCI01000106.1.
DR PDB; 2FXQ; X-ray; 1.85 A; A=1-264.
DR PDB; 2IHE; X-ray; 2.10 A; A=1-264.
DR PDB; 2IHF; X-ray; 1.90 A; A=1-264.
DR PDBsum; 2FXQ; -.
DR PDBsum; 2IHE; -.
DR PDBsum; 2IHF; -.
DR AlphaFoldDB; Q9KH06; -.
DR SMR; Q9KH06; -.
DR EvolutionaryTrace; Q9KH06; -.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR CDD; cd04496; SSB_OBF; 2.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_00984; SSB; 2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR000424; Primosome_PriB/ssb.
DR InterPro; IPR011344; ssDNA-bd.
DR PANTHER; PTHR10302; PTHR10302; 2.
DR Pfam; PF00436; SSB; 2.
DR SUPFAM; SSF50249; SSF50249; 2.
DR TIGRFAMs; TIGR00621; ssb; 2.
DR PROSITE; PS50935; SSB; 2.
PE 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA recombination; DNA repair; DNA replication;
KW DNA-binding; Repeat.
FT CHAIN 1..264
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096148"
FT DOMAIN 5..108
FT /note="SSB 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DOMAIN 128..228
FT /note="SSB 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 224..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 259..264
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:2IHF"
FT STRAND 28..41
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 47..59
FT /evidence="ECO:0007829|PDB:2FXQ"
FT HELIX 61..66
FT /evidence="ECO:0007829|PDB:2FXQ"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 97..106
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 129..139
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2IHF"
FT STRAND 151..160
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:2FXQ"
FT HELIX 180..186
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:2FXQ"
FT STRAND 213..225
FT /evidence="ECO:0007829|PDB:2FXQ"
SQ SEQUENCE 264 AA; 30029 MW; CF0AB49B5AA6A454 CRC64;
MARGLNQVFL IGTLTARPDM RYTPGGLAIL DLNLAGQDAF TDESGQEREV PWYHRVRLLG
RQAEMWGDLL EKGQLIFVEG RLEYRQWEKD GEKKSEVQVR AEFIDPLEGR GRETLEDARG
QPRLRRALNQ VILMGNLTRD PDLRYTPQGT AVVRLGLAVN ERRRGQEEER THFLEVQAWR
ELAEWASELR KGDGLLVIGR LVNDSWTSSS GERRFQTRVE ALRLERPTRG PAQAGGSRPP
TVQTGGVDID EGLEDFPPEE DLPF