ID   SSB_STAAR               Reviewed;         156 AA.
AC   Q6GF73;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 104.
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=SAR2083;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG41066.1; -; Genomic_DNA.
DR   RefSeq; WP_000934764.1; NC_002952.2.
DR   AlphaFoldDB; Q6GF73; -.
DR   SMR; Q6GF73; -.
DR   KEGG; sar:SAR2083; -.
DR   HOGENOM; CLU_078758_6_1_9; -.
DR   OMA; INIVIWR; -.
DR   OrthoDB; 1942216at2; -.
DR   Proteomes; UP000000596; 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..156
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096102"
FT   DOMAIN          1..104
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          104..156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           151..156
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        104..138
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   156 AA;  17627 MW;  9BC648903DC8B1B3 CRC64;
     MLNRTILVGR LTRDPELRTT QSGVNVASFT LAVNRTFTNA QGEREADFIN IIVFKKQAEN
     VNKYLSKGSL AGVDGRLQTR NYENKEGQRV YVTEVVADSI QFLEPKNSND TQQDLYQQQV
     QQTRGQSQYS NNKPVKDNPF ANANGPIELN DDDLPF