ID   SSB_STRP3               Reviewed;         163 AA.
AC   P0DF76; P66853; Q99Y80;
DT   27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 1.
DT   25-MAY-2022, entry version 53.
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=SpyM3_1581;
OS   Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=198466;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-595 / MGAS315;
RX   PubMed=12122206; DOI=10.1073/pnas.152298499;
RA   Beres S.B., Sylva G.L., Barbian K.D., Lei B., Hoff J.S., Mammarella N.D.,
RA   Liu M.-Y., Smoot J.C., Porcella S.F., Parkins L.D., Campbell D.S.,
RA   Smith T.M., McCormick J.K., Leung D.Y.M., Schlievert P.M., Musser J.M.;
RT   "Genome sequence of a serotype M3 strain of group A Streptococcus: phage-
RT   encoded toxins, the high-virulence phenotype, and clone emergence.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:10078-10083(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: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00984}.
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DR   EMBL; AE014074; AAM80188.1; -; Genomic_DNA.
DR   RefSeq; WP_002983122.1; NC_004070.1.
DR   AlphaFoldDB; P0DF76; -.
DR   SMR; P0DF76; -.
DR   EnsemblBacteria; AAM80188; AAM80188; SpyM3_1581.
DR   GeneID; 57853239; -.
DR   KEGG; spg:SpyM3_1581; -.
DR   HOGENOM; CLU_078758_6_2_9; -.
DR   OMA; SGSVKCR; -.
DR   Proteomes; UP000000564; 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.
FT   CHAIN           1..163
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096119"
FT   DOMAIN          1..104
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          109..163
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           158..163
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        109..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   163 AA;  17982 MW;  1AA961F3522CFB58 CRC64;
     MINNVVLVGR MTKDAELRYT PSQVAVATFT LAVNRTFKSQ NGEREADFIN CVIWRQPAEN
     LANWAKKGAL IGVTGRIQTR NYENQQGQRV YVTEVVADNF QMLESRATRE GGSTGSFNGG
     FNNNTSSSNS YSAPAQQTPN FGRDDSPFGN SNPMDISDDD LPF