SSB_DEIRA
ID SSB_DEIRA Reviewed; 301 AA.
AC Q9RY51;
DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2003, sequence version 2.
DT 25-MAY-2022, entry version 135.
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; OrderedLocusNames=DR_0099;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBUNIT.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=14718065; DOI=10.1186/1471-2180-4-2;
RA Eggington J.M., Haruta N., Wood E.A., Cox M.M.;
RT "The single-stranded DNA-binding protein of Deinococcus radiodurans.";
RL BMC Microbiol. 4:2-2(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, AND DNA-BINDING.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15781492; DOI=10.1093/nar/gki310;
RA Witte G., Urbanke C., Curth U.;
RT "Single-stranded DNA-binding protein of Deinococcus radiodurans: a
RT biophysical characterization.";
RL Nucleic Acids Res. 33:1662-1670(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [4]
RP FUNCTION AS AN SSB PROTEIN, AND DNA-BINDING.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15466873; DOI=10.1074/jbc.m408645200;
RA Wang J., Julin D.A.;
RT "DNA helicase activity of the RecD protein from Deinococcus radiodurans.";
RL J. Biol. Chem. 279:52024-52032(2004).
RN [5]
RP FUNCTION, AND INTERACTION WITH DDRB.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=20451472; DOI=10.1016/j.dnarep.2010.04.006;
RA Xu G., Lu H., Wang L., Chen H., Xu Z., Hu Y., Tian B., Hua Y.;
RT "DdrB stimulates single-stranded DNA annealing and facilitates RecA-
RT independent DNA repair in Deinococcus radiodurans.";
RL DNA Repair 9:805-812(2010).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=23951213; DOI=10.1371/journal.pone.0071651;
RA Lockhart J.S., DeVeaux L.C.;
RT "The essential role of the Deinococcus radiodurans ssb gene in cell
RT survival and radiation tolerance.";
RL PLoS ONE 8:E71651-E71651(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS), AND SUBUNIT.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=15159541; DOI=10.1073/pnas.0401331101;
RA Bernstein D.A., Eggington J.M., Killoran M.P., Misic A.M., Cox M.M.,
RA Keck J.L.;
RT "Crystal structure of the Deinococcus radiodurans single-stranded DNA-
RT binding protein suggests a mechanism for coping with DNA damage.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:8575-8580(2004).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 290-301.
RA George N.P., Keck J.L.;
RT "Identification of the SSB-interaction platform of Deinococcus radiodurans
RT uracil-DNA glycosylase.";
RL Submitted (NOV-2011) to the PDB data bank.
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SSDNA, SUBUNIT,
RP SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=22570477; DOI=10.1074/jbc.m112.367573;
RA George N.P., Ngo K.V., Chitteni-Pattu S., Norais C.A., Battista J.R.,
RA Cox M.M., Keck J.L.;
RT "Structure and cellular dynamics of Deinococcus radiodurans single-stranded
RT DNA (ssDNA)-binding protein (SSB)-DNA complexes.";
RL J. Biol. Chem. 287:22123-22132(2012).
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 (By similarity).
CC Essential for ionizing radiation resistance. Stimulates the 5'-3' DNA
CC helicase activity of RecD-like helicase. Stimulates RecA protein-
CC promoted DNA three-strand exchange reactions in vitro with both
CC D.radiodurans and E.coli-derived RecA. Complements an ssb deletion in
CC E.coli, but does not complement a ddrb disruption in D.radiodurans.
CC {ECO:0000255|HAMAP-Rule:MF_00984, ECO:0000269|PubMed:14718065,
CC ECO:0000269|PubMed:15466873, ECO:0000269|PubMed:20451472,
CC ECO:0000269|PubMed:23951213}.
CC -!- SUBUNIT: Homodimer. Binds ssDNA. Interacts with DdrB.
CC {ECO:0000269|PubMed:14718065, ECO:0000269|PubMed:15159541,
CC ECO:0000269|PubMed:15781492, ECO:0000269|PubMed:20451472,
CC ECO:0000269|PubMed:22570477}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22570477}.
CC Note=During log phase, present in multiple foci. 1 hour after
CC irradiation most foci are condensed in the center of the cell's
CC nucleoid, they dissipate by 2 hours later.
CC -!- INDUCTION: Constitutively expressed, highly up-regulated following
CC ionizing radiation for at least 12 hours (at protein level).
CC {ECO:0000269|PubMed:22570477}.
CC -!- DISRUPTION PHENOTYPE: Essential, it cannot be knocked out. As SSB
CC levels are depleted growth slows, tolerance to ionizing radiation and
CC UV light decreases rapidly. Cannot be complemented by ddrB.
CC {ECO:0000269|PubMed:23951213}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF09692.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY293617; AAQ18705.1; -; Genomic_DNA.
DR EMBL; AJ564860; CAD92322.1; -; Genomic_DNA.
DR EMBL; AE000513; AAF09692.1; ALT_FRAME; Genomic_DNA.
DR PIR; A75559; A75559.
DR RefSeq; NP_293825.1; NC_001263.1.
DR RefSeq; WP_027480308.1; NZ_CP015081.1.
DR PDB; 1SE8; X-ray; 1.80 A; A=1-301.
DR PDB; 3UDG; X-ray; 2.40 A; A/B/C=1-301.
DR PDB; 3UFM; X-ray; 1.95 A; B=290-301.
DR PDBsum; 1SE8; -.
DR PDBsum; 3UDG; -.
DR PDBsum; 3UFM; -.
DR AlphaFoldDB; Q9RY51; -.
DR SMR; Q9RY51; -.
DR STRING; 243230.DR_0099; -.
DR EnsemblBacteria; AAF09692; AAF09692; DR_0099.
DR KEGG; dra:DR_0099; -.
DR PATRIC; fig|243230.17.peg.263; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_1802971_0_0_0; -.
DR InParanoid; Q9RY51; -.
DR OMA; ARGMNHV; -.
DR OrthoDB; 1942216at2; -.
DR EvolutionaryTrace; Q9RY51; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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 GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
DR CDD; cd04496; SSB_OBF; 2.
DR Gene3D; 2.40.50.140; -; 2.
DR HAMAP; MF_00984; SSB; 1.
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; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA replication; DNA-binding; Reference proteome; Repeat.
FT CHAIN 1..301
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096147"
FT DOMAIN 5..110
FT /note="SSB 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT DOMAIN 129..232
FT /note="SSB 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 238..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 296..301
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT COMPBIAS 246..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 28..39
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1SE8"
FT HELIX 61..68
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 76..88
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 96..108
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 143..146
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 152..165
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 171..183
FT /evidence="ECO:0007829|PDB:1SE8"
FT HELIX 185..190
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 198..209
FT /evidence="ECO:0007829|PDB:1SE8"
FT STRAND 219..230
FT /evidence="ECO:0007829|PDB:1SE8"
SQ SEQUENCE 301 AA; 32722 MW; 21B2090C970E1B0E CRC64;
MARGMNHVYL IGALARDPEL RYTGNGMAVF EATVAGEDRV IGNDGRERNL PWYHRVSILG
KPAEWQAERN LKGGDAVVVE GTLEYRQWEA PEGGKRSAVN VKALRMEQLG TQPELIQDAG
GGVRMSGAMN EVLVLGNVTR DPEIRYTPAG DAVLSLSIAV NENYQDRQGQ RQEKVHYIDA
TLWRDLAENM KELRKGDPVM IMGRLVNEGW TDKDGNKRNS TRVEATRVEA LARGAGNANS
GYAAATPAAP RTQTASSAAR PTSGGYQSQP SRAANTGSRS GGLDIDQGLD DFPPEEDDLP
F
