ID   F2LCY9_BURGS            Unreviewed;       198 AA.
AC   F2LCY9;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   18-JUN-2025, entry version 78.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|HAMAP-Rule:MF_00984, ECO:0000256|RuleBase:RU000524};
DE            Short=SSB {ECO:0000256|HAMAP-Rule:MF_00984};
GN   OrderedLocusNames=bgla_1g34730 {ECO:0000313|EMBL:AEA62076.1};
OS   Burkholderia gladioli (strain BSR3).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=999541 {ECO:0000313|EMBL:AEA62076.1, ECO:0000313|Proteomes:UP000008316};
RN   [1] {ECO:0000313|EMBL:AEA62076.1, ECO:0000313|Proteomes:UP000008316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BSR3 {ECO:0000313|EMBL:AEA62076.1,
RC   ECO:0000313|Proteomes:UP000008316};
RX   PubMed=21478339; DOI=10.1128/JB.00420-11;
RA   Seo Y.S., Lim J., Choi B.S., Kim H., Goo E., Lee B., Lim J.S., Choi I.Y.,
RA   Moon J.S., Kim J., Hwang I.;
RT   "Complete genome sequence of Burkholderia gladioli BSR3.";
RL   J. Bacteriol. 193:3149-3149(2011).
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:0000256|HAMAP-Rule:MF_00984}.
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|HAMAP-Rule:MF_00984}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00984}.
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DR   EMBL; CP002599; AEA62076.1; -; Genomic_DNA.
DR   RefSeq; WP_013699393.1; NC_015381.1.
DR   AlphaFoldDB; F2LCY9; -.
DR   STRING; 999541.bgla_1g34730; -.
DR   GeneID; 66459182; -.
DR   KEGG; bgd:bgla_1g34730; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_1_4; -.
DR   Proteomes; UP000008316; Chromosome 1.
DR   GO; GO:0009295; C:nucleoid; IEA:TreeGrafter.
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; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
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   NCBIfam; NF005406; PRK06958.1; 1.
DR   NCBIfam; TIGR00621; ssb; 1.
DR   PANTHER; PTHR10302; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   PANTHER; PTHR10302:SF27; SINGLE-STRANDED DNA-BINDING PROTEIN; 1.
DR   Pfam; PF00436; SSB; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00984};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00984}; Reference proteome {ECO:0000313|Proteomes:UP000008316}.
FT   REGION          137..198
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           193..198
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00984"
FT   COMPBIAS        137..177
FT                   /note="Gly residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   198 AA;  19750 MW;  CFB6294A29218258 CRC64;
     MASVNKVILV GNLGADPEVR YLPSGDAVAN IRLATTDRYK DKATNEFKEV TEWHRVAFFG
     RLAEIVNEYL KKGSAVYIEG RLRTRKWQGQ DGQDRYSTEI VADQMQMLGG RGGAGGGGGG
     GDDGYGGGGG GGYGGGSGGG GGGYGGGRGG DMERGGGGGG RASGGGGARS GGGGGGSSRP
     SQPASGGGFD EMDDDIPF
//