ID   SSB_ECOL6               Reviewed;         178 AA.
AC   P0AGE1; P02339;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 90.
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=c5049;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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; AE014075; AAN83475.1; -; Genomic_DNA.
DR   RefSeq; WP_000168305.1; NC_004431.1.
DR   AlphaFoldDB; P0AGE1; -.
DR   BMRB; P0AGE1; -.
DR   SMR; P0AGE1; -.
DR   STRING; 199310.c5049; -.
DR   EnsemblBacteria; AAN83475; AAN83475; c5049.
DR   GeneID; 66672025; -.
DR   KEGG; ecc:c5049; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_2_6; -.
DR   OMA; GQMQERT; -.
DR   BioCyc; ECOL199310:C5049-MON; -.
DR   Proteomes; UP000001410; 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   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..178
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096038"
FT   DOMAIN          6..111
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   DNA_BIND        55..61
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          113..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           173..178
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        133..161
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   178 AA;  18975 MW;  F0AF43B6DC8D02FC CRC64;
     MASRGVNKVI LVGNLGQDPE VRYMPNGGAV ANITLATSES WRDKATGEMK EQTEWHRVVL
     FGKLAEVASE YLRKGSQVYI EGQLRTRKWT DQSGQDRYTT EVVVNVGGTM QMLGGRQGGG
     APAGGNIGGG QPQGGWGQPQ QPQGGNQFSG GAQSRPQQSA PAAPSNEPPM DFDDDIPF