ID   SSB_XANCP               Reviewed;         172 AA.
AC   Q8P778;
DT   24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 107.
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=XCC2735;
OS   Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB
OS   528 / LMG 568 / P 25).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=190485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25;
RX   PubMed=12024217; DOI=10.1038/417459a;
RA   da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA   Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA   Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA   Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA   Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA   Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA   Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA   Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA   Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA   Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA   Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA   Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA   Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA   Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT   "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT   specificities.";
RL   Nature 417:459-463(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; AE008922; AAM42007.1; -; Genomic_DNA.
DR   RefSeq; NP_638083.1; NC_003902.1.
DR   RefSeq; WP_011037865.1; NC_003902.1.
DR   AlphaFoldDB; Q8P778; -.
DR   SMR; Q8P778; -.
DR   STRING; 340.xcc-b100_1426; -.
DR   EnsemblBacteria; AAM42007; AAM42007; XCC2735.
DR   KEGG; xcc:XCC2735; -.
DR   PATRIC; fig|190485.4.peg.2920; -.
DR   eggNOG; COG0629; Bacteria.
DR   HOGENOM; CLU_078758_0_2_6; -.
DR   OMA; GQMQERT; -.
DR   Proteomes; UP000001010; Chromosome.
DR   GO; GO:0009295; C:nucleoid; IBA:GO_Central.
DR   GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
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   GO; GO:0051096; P:positive regulation of helicase activity; IBA:GO_Central.
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..172
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000096142"
FT   DOMAIN          5..109
FT                   /note="SSB"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT   REGION          107..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           167..172
FT                   /note="Important for interaction with partner proteins"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
SQ   SEQUENCE   172 AA;  18633 MW;  ABE9BED107B9BAD6 CRC64;
     MARGINKVIL VGNLGNDPDT KYTQAGMAIT RVSLATTSMR KDREGNNQER TEWHRVVFFG
     KLGEIAGEYL RKGSQVYVEG ELRYDKYTGQ DGVEKYSTDI VANEMQMLGG RGEGGGGGGM
     GGDRPQRTQA PRQQQGGGGG GGGQDYAPRR QQPAQQQSAP PMDDFADDDI PF