ID   SSB_BPT3                Reviewed;         232 AA.
AC   P20313;
DT   01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1991, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04153};
DE            Short=SSB protein {ECO:0000255|HAMAP-Rule:MF_04153};
DE   AltName: Full=Helix-destabilizing protein {ECO:0000255|HAMAP-Rule:MF_04153};
GN   Name=2.5;
OS   Enterobacteria phage T3 (Bacteriophage T3).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC   Escherichia virus T3.
OX   NCBI_TaxID=10759;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Luria;
RX   PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2;
RA   Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.;
RT   "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9.";
RL   J. Mol. Biol. 210:687-701(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-181.
RX   PubMed=3586029; DOI=10.1016/0022-2836(87)90261-0;
RA   Schmitt M.P., Beck P.J., Kearney C.A., Spence J.L., Digiovanni D.,
RA   Condreay J.P., Molineux I.J.;
RT   "Sequence of a conditionally essential region of bacteriophage T3,
RT   including the primary origin of DNA replication.";
RL   J. Mol. Biol. 193:479-495(1987).
CC   -!- FUNCTION: Single-stranded DNA-binding protein that participates in
CC       viral DNA replication, formation of concatemers, recombination and
CC       repair of double-stranded breaks. Coats the lagging-strand ssDNA as the
CC       replication fork advances and stimulates the activities of viral DNA
CC       polymerase and primase/helicase. Coordinates simultaneous synthesis of
CC       leading- and lagging-strands. Together with DNA primase/helicase,
CC       promotes pairing of two homologous DNA molecules containing
CC       complementary single-stranded regions and mediates homologous DNA
CC       strand exchange. Promotes also the formation of joint molecules.
CC       Disrupts loops, hairpins and other secondary structures present on
CC       ssDNA to reduce and eliminate pausing of viral DNA polymerase at
CC       specific sites during elongation. {ECO:0000255|HAMAP-Rule:MF_04153}.
CC   -!- SUBUNIT: Homodimer. Interacts (via C-terminus) with the viral DNA
CC       polymerase. Interacts with the viral helicase/primase. Part of the
CC       replicase complex that includes the DNA polymerase, the
CC       primase/helicase and the single-stranded DNA binding protein.
CC       {ECO:0000255|HAMAP-Rule:MF_04153}.
CC   -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC       binding properties. It is also required for dimer formation and for
CC       interactions with the viral DNA polymerase and the helicase.
CC       {ECO:0000255|HAMAP-Rule:MF_04153}.
CC   -!- SIMILARITY: Belongs to the Teseptimavirus single-stranded DNA-binding
CC       protein family. {ECO:0000255|HAMAP-Rule:MF_04153}.
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DR   EMBL; X17255; CAA35131.1; -; Genomic_DNA.
DR   EMBL; X05031; CAA28706.1; -; Genomic_DNA.
DR   PIR; S07504; S07504.
DR   RefSeq; NP_523311.1; NC_003298.1.
DR   SMR; P20313; -.
DR   GeneID; 927413; -.
DR   KEGG; vg:927413; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; 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.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_04153; SSB_T7; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR016411; SSB_T7.
DR   PIRSF; PIRSF004311; Helix_destablz_SSB_T7; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   Viral DNA replication.
FT   CHAIN           1..232
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000106482"
FT   REGION          190..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          213..232
FT                   /note="Dimerization and interaction with the viral DNA
FT                   polymerase and helicase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_04153"
FT   COMPBIAS        202..216
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..232
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   232 AA;  25907 MW;  D28C71357275BB35 CRC64;
     MAGFKKKVYT SGLGTAEPYA YLSKPDYGNE ERGFGNPRGV YKVDLTLSNK DPRCQAMVDE
     IVKTHEEAYA AAVEEFEANP PQVQRGKKPL TPYEGDMPFF DNGDGTTTFK FKCYASFQDK
     KTKETKHINL VVVDSKGKKI QEVPIIGGGS KLKVKYSLVP YKWNTAVGAS VKLQLESVML
     VELATFGGGG EDEWADEVED GGYTASESRQ SRDEQEWQED EHEETPDDDE DF