ID   SSB_BUCAI               Reviewed;         171 AA.
AC   P57610;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   25-MAY-2022, entry version 114.
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=BU545;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13237.1; -; Genomic_DNA.
DR   RefSeq; NP_240351.1; NC_002528.1.
DR   RefSeq; WP_009874495.1; NC_002528.1.
DR   AlphaFoldDB; P57610; -.
DR   SMR; P57610; -.
DR   STRING; 107806.10039203; -.
DR   EnsemblBacteria; BAB13237; BAB13237; BAB13237.
DR   KEGG; buc:BU545; -.
DR   PATRIC; fig|107806.10.peg.549; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_2_6; -.
DR   OMA; SGSVKCR; -.
DR   Proteomes; UP000001806; 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   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..171
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096017"
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          150..171
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           166..171
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   COMPBIAS        150..165
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   171 AA;  19356 MW;  1DEEBDCF08CAFADA CRC64;
     MASRGVNKVI LIGHLGQDPE VRYMPNGNAV VNMTLATSEN WKDKNTGENK EKTEWHRIVL
     FGKLAEIAGE YLRKGSQVYI EGSLQTRKWQ DQNGLERYTT EIIVNIGGTM QMLGNRNSNL
     QAMTVNDKNS TGIKIKKTDA VEFDKKIETH ESNKDLTHSP SEIDFDDEIP F