ID   SSB_BPGA1               Reviewed;         170 AA.
AC   Q9MCD0;
DT   11-MAY-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 47.
DE   RecName: Full=Single-stranded DNA-binding protein;
DE            Short=SSB;
DE   AltName: Full=Gene product 5;
DE            Short=gp5;
DE   AltName: Full=Protein p5;
GN   Name=gene 5 {ECO:0000312|EMBL:CAC21526.1};
OS   Bacillus phage GA-1 (Bacteriophage GA-1).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Salasmaviridae; Tatarstanvirinae; Gaunavirus.
OX   NCBI_TaxID=2679898;
OH   NCBI_TaxID=1423; Bacillus subtilis.
RN   [1] {ECO:0000312|EMBL:CAC21526.1, ECO:0000312|Proteomes:UP000002580}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Meijer W.J.J., Horcajadas J.A., Salas M.;
RT   "The phi29 family of phages.";
RL   Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION.
RX   PubMed=10773070; DOI=10.1093/nar/28.10.2034;
RA   Gascon I., Lazaro J.M., Salas M.;
RT   "Differential functional behavior of viral phi29, Nf and GA-1 SSB
RT   proteins.";
RL   Nucleic Acids Res. 28:2034-2042(2000).
RN   [3]
RP   SUBUNIT.
RX   PubMed=10686098; DOI=10.1006/jmbi.2000.3521;
RA   Gascon I., Gutierrez C., Salas M.;
RT   "Structural and functional comparative study of the complexes formed by
RT   viral phi29, Nf and GA-1 SSB proteins with DNA.";
RL   J. Mol. Biol. 296:989-999(2000).
RN   [4]
RP   DOMAIN.
RX   PubMed=11956216; DOI=10.1074/jbc.m202430200;
RA   Gascon I., Carrascosa J.L., Villar L., Lazaro J.M., Salas M.;
RT   "Importance of the N-terminal region of the phage GA-1 single-stranded DNA-
RT   binding protein for its self-interaction ability and functionality.";
RL   J. Biol. Chem. 277:22534-22540(2002).
CC   -!- FUNCTION: Single-stranded DNA-binding protein required for the
CC       elongation during viral DNA replication by strand displacement.
CC       Displaced viral DNA strands are transiently coated with the ssDNA-
CC       binding protein and therefore protected againt nucleases. The latter is
CC       then probably removed by the replisome that performs lagging strand
CC       synthesis or during the events that lead up to the recombination
CC       process. Has helix-destabilizing activity since it removes secondary
CC       structure from the ssDNA in replicative intermediates.
CC       {ECO:0000305|PubMed:10773070}.
CC   -!- SUBUNIT: Hexamer. {ECO:0000269|PubMed:10686098}.
CC   -!- DOMAIN: The N-terminus is required for oligomerization.
CC       {ECO:0000269|PubMed:11956216}.
CC   -!- SIMILARITY: Belongs to the phi29likevirus single-strand-binding protein
CC       family. {ECO:0000305}.
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DR   EMBL; X96987; CAC21526.1; -; Genomic_DNA.
DR   RefSeq; NP_073688.1; NC_002649.1.
DR   GeneID; 919894; -.
DR   KEGG; vg:919894; -.
DR   Proteomes; UP000002580; Genome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   DNA replication; DNA-binding; Early protein; Reference proteome;
KW   Viral DNA replication.
FT   CHAIN           1..170
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000436076"
FT   REGION          1..26
FT                   /note="Oligomerization"
FT                   /evidence="ECO:0000269|PubMed:11956216"
SQ   SEQUENCE   170 AA;  19155 MW;  DCBD99E01FE38F16 CRC64;
     MSNELKQVEQ TEEAVVVSET KDYIKVYENG KYRRKAKYQQ LNSMSHRELT DEEEINIFNL
     LNGAEGSAVE MKRAVGSKVT IVDFITVPYT KIDEDTGVEE NGVLTYLINE NGEAIATSSK
     AVYFTLNRLL IQCGKHADGT WKRPIVEIIS VKQTNGDGMD LKLVGFDKKK