SSB_BUCBP
ID SSB_BUCBP Reviewed; 166 AA.
AC Q89A53;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
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=bbp_488;
OS Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=224915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bp;
RX PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT "Reductive genome evolution in Buchnera aphidicola.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27193.1; -; Genomic_DNA.
DR RefSeq; WP_011091594.1; NC_004545.1.
DR AlphaFoldDB; Q89A53; -.
DR SMR; Q89A53; -.
DR STRING; 224915.bbp_488; -.
DR PRIDE; Q89A53; -.
DR EnsemblBacteria; AAO27193; AAO27193; bbp_488.
DR GeneID; 56471023; -.
DR KEGG; bab:bbp_488; -.
DR eggNOG; COG0629; Bacteria.
DR HOGENOM; CLU_078758_0_2_6; -.
DR OMA; SGSVKCR; -.
DR OrthoDB; 1942216at2; -.
DR Proteomes; UP000000601; 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;
KW Reference proteome.
FT CHAIN 1..166
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000096019"
FT DOMAIN 6..111
FT /note="SSB"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
FT REGION 143..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 161..166
FT /note="Important for interaction with partner proteins"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00984"
SQ SEQUENCE 166 AA; 18717 MW; 587B1D9ADBB30D82 CRC64;
MASRGINKVI LIGYLGQDPD VRYMQNGSAV TNITLATSET WKDKNNGEIK EKTEWHRIVF
FNKLAEIAGE YLKKGSQVYI EGSLQTRKWK DQNGIERYIT EIIVSVGGTM QMLGSRNSSS
LTASSGLSKN NDNLSKQLLS EKKQESFNDS KLQNNNLDFD DEDIPF