ID   SSB_BPR70               Reviewed;         117 AA.
AC   O21945;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 70.
DE   RecName: Full=Single-stranded DNA-binding protein;
DE            Short=SSB protein;
DE   AltName: Full=Gp32;
DE   AltName: Full=Helix-destabilizing protein;
DE   Flags: Fragment;
GN   Name=32; Synonyms=ssb;
OS   Enterobacteria phage RB70 (Bacteriophage RB70).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus;
OC   unclassified Tequatrovirus.
OX   NCBI_TaxID=36338;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Theimer C.A., Krisch H.M., Giedroc D.P.;
RL   Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Single-stranded DNA-binding protein that participates in
CC       viral DNA replication, recombination, and repair. Coats the lagging-
CC       strand ssDNA as the replication fork advances. Stimulates the
CC       activities of viral DNA polymerase and DnaB-like SF4 replicative
CC       helicase, probably via its interaction with the helicase assembly
CC       factor. Together with DnaB-like SF4 replicative helicase and the
CC       helicase assembly factor, promotes pairing of two homologous DNA
CC       molecules containing complementary single-stranded regions and mediates
CC       homologous DNA strand exchange. Promotes also the formation of joint
CC       molecules. mRNA specific autogenous translational repressor.
CC       {ECO:0000250|UniProtKB:P03695}.
CC   -!- SUBUNIT: Homodimer in the absence of DNA, monomer when binding DNA.
CC       Interacts with the DNA helicase assembly protein; a ternary complex
CC       between the helicase assembly protein, the single-stranded DNA-binding
CC       protein and ssDNA is an obligatory intermediate in the helicase loading
CC       mechanism. Part of the replicase complex that includes the DNA
CC       polymerase, the polymerase clamp, the clamp loader complex, the single-
CC       stranded DNA binding protein, the primase, the DnaB-like SF4
CC       replicative helicase and the helicase assembly factor. Interacts (via
CC       C-terminus) with the viral SF1 dDA helicase. Interacts with the viral
CC       SF2 UvsW repair helicase. {ECO:0000250|UniProtKB:P03695}.
CC   -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC       binding properties. The N-terminus LAST motif is involved in the
CC       cooperative binding of the protein to ssDNA.
CC       {ECO:0000250|UniProtKB:P03695}.
CC   -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding
CC       protein family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF033317; AAB87483.1; -; Genomic_DNA.
DR   SMR; O21945; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; 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; 3.90.198.10; -; 1.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR012339; Phage_T4_Gp32_ssDNA-bd.
DR   InterPro; IPR044947; Phage_T4_Gp32_ssDNA-bd_sf.
DR   Pfam; PF08804; gp32; 1.
DR   SUPFAM; SSF50249; SSF50249; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; DNA replication; DNA-binding;
KW   Metal-binding; Repressor; Viral DNA replication; Zinc.
FT   CHAIN           1..>117
FT                   /note="Single-stranded DNA-binding protein"
FT                   /id="PRO_0000165063"
FT   REGION          3..7
FT                   /note="LAST"
FT                   /evidence="ECO:0000250|UniProtKB:P03695"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03695"
FT   BINDING         78
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03695"
FT   BINDING         88
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03695"
FT   BINDING         91
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250|UniProtKB:P03695"
FT   NON_TER         117
SQ   SEQUENCE   117 AA;  13207 MW;  EE3073DE19A4804F CRC64;
     MFKRKSTAEL AAQMAKLAGN KGGFSSEDKG EWKLKLDNAG NGQAVIRFLP SKNDEQAPFA
     ILVNHGFKKN GKWYIENCSS THGDYDSCPV CQYISKNDLY NTDNKEYGLV KRKTSYW