ID   SSB1_LACLA              Reviewed;         150 AA.
AC   Q9CGS5;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 112.
DE   RecName: Full=Single-stranded DNA-binding protein 1 {ECO:0000255|HAMAP-Rule:MF_00984};
DE            Short=SSB 1 {ECO:0000255|HAMAP-Rule:MF_00984};
GN   Name=ssb1; OrderedLocusNames=LL1019; ORFNames=L0300;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
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: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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DR   EMBL; AE005176; AAK05117.1; -; Genomic_DNA.
DR   PIR; C86752; C86752.
DR   RefSeq; NP_267175.1; NC_002662.1.
DR   RefSeq; WP_010905690.1; NC_002662.1.
DR   AlphaFoldDB; Q9CGS5; -.
DR   SMR; Q9CGS5; -.
DR   STRING; 272623.L0300; -.
DR   PaxDb; Q9CGS5; -.
DR   EnsemblBacteria; AAK05117; AAK05117; L0300.
DR   KEGG; lla:L0300; -.
DR   PATRIC; fig|272623.7.peg.1090; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_6_2_9; -.
DR   OMA; RFRDSNH; -.
DR   Proteomes; UP000002196; Chromosome.
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; -; 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   PANTHER; PTHR10302; PTHR10302; 1.
DR   Pfam; PF00436; SSB; 1.
DR   PIRSF; PIRSF002070; SSB; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   TIGRFAMs; TIGR00621; ssb; 1.
DR   PROSITE; PS50935; SSB; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW   Reference proteome.
FT   CHAIN           1..150
FT                   /note="Single-stranded DNA-binding protein 1"
FT                   /id="PRO_0000096052"
FT   DOMAIN          1..104
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          103..150
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           145..150
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        103..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   150 AA;  16644 MW;  E8EFB78A41676E8C CRC64;
     MINNVVLVGR LTRDPELRHT PQNQAVGTFG LAVNRQFKNA NGEREADFIN CVIWRQQAEN
     LAKFAKKGAL IGITGRIQTR NYENQQGQKV YVTEVVADTF QMLESNKTQG QQTSKPQAQN
     KKPQAPDPFK APAADPFAGG TEISDDDLPF