ID   SSB2_LACLA              Reviewed;         166 AA.
AC   Q9CDM9;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Single-stranded DNA-binding protein 2 {ECO:0000255|HAMAP-Rule:MF_00984};
DE            Short=SSB 2 {ECO:0000255|HAMAP-Rule:MF_00984};
GN   Name=ssb2; OrderedLocusNames=LL2190; ORFNames=L0302;
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; AAK06288.1; -; Genomic_DNA.
DR   PIR; F86898; F86898.
DR   RefSeq; NP_268347.1; NC_002662.1.
DR   RefSeq; WP_003131953.1; NC_002662.1.
DR   AlphaFoldDB; Q9CDM9; -.
DR   SMR; Q9CDM9; -.
DR   STRING; 272623.L0302; -.
DR   PaxDb; Q9CDM9; -.
DR   EnsemblBacteria; AAK06288; AAK06288; L0302.
DR   GeneID; 66443182; -.
DR   KEGG; lla:L0302; -.
DR   PATRIC; fig|272623.7.peg.2352; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_6_2_9; -.
DR   OMA; INIVIWR; -.
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..166
FT                   /note="Single-stranded DNA-binding protein 2"
FT                   /id="PRO_0000096053"
FT   DOMAIN          1..104
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          108..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           161..166
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        118..145
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   166 AA;  18304 MW;  054B5F6BA4851769 CRC64;
     MINNVVLVGR ITRDPELRYT PQNQAVATFS LAVNRQFKNA NGEREADFIN CVIWRQQAEN
     LANWAKKGAL IGVTGRIQTR NYENQQGQRV YVTEVVADSF QMLESRSARE GMGGGTSAGS
     YSAPSQSTNN TPRPQTNNNN ATPNFGRDAD PFGSSPMEIS DDDLPF