AC   MF_04152;
DC   Protein; auto
TR   HAMAP; MF_04152; -; 1; level=0
XX
Names: SSB_T4
XX
ID   SSB
case <OC:Tequatrovirus>
DE   RecName: Full=Single-stranded DNA-binding protein;
DE            Short=SSB protein;
DE   AltName: Full=Gp32;
DE   AltName: Full=Helix-destabilizing protein;
GN   Name=32; Synonyms=ssb;
else
DE   RecName: Full=Single-stranded DNA-binding protein;
DE            Short=SSB protein;
DE   AltName: Full=Helix-destabilizing protein;
end case
XX
case <OC:Tequatrovirus>
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   -!- 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.
CC   -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding
CC       protein family.
else
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 the replicative helicase,
CC       probably via its interaction with the helicase assembly factor.
CC       Together with the replicative helicase and the helicase assembly
CC       factor, 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. mRNA
CC       specific autogenous translational repressor.
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 replicative helicase and
CC       the helicase assembly factor. Interacts (via C-terminus) with the viral
CC       SF1 dDA helicase. Interacts with the viral SF2 UvsW repair helicase.
CC   -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC       binding properties. The N-terminus LAST motif is
CC       involved in the cooperative binding of the protein to single-stranded
CC       nucleic acids.
CC   -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding
CC       protein family.
end case
case <FTTag:LAST>
CC   -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC       binding properties. The N-terminus LAST motif is
CC       involved in the cooperative binding of the protein to ssDNA.
else
CC   -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC       binding properties.
end case
XX
DR   Pfam; PF08804; gp32; 1; trigger=no
XX
KW   DNA recombination
KW   DNA repair
KW   DNA-binding
KW   Repressor
KW   Viral DNA replication
case <FTGroup:1>
KW   Metal-binding
KW   Zinc
end case
XX
case <FTGroup:1>
GO   GO:0046872; F:metal ion binding
end case
GO   GO:0003697; F:single-stranded DNA binding
GO   GO:0039686; P:bidirectional double-stranded viral DNA replication
GO   GO:0006310; P:DNA recombination
GO   GO:0006281; P:DNA repair
GO   GO:0039693; P:viral DNA genome replication
XX
FT   From: SSB_BPT4 (P03695)
FT   REGION          3..7
FT                   /note="LAST"
FT   Tag: LAST; Optional; Condition: [KR]-[KR]-[KR]-x-x
FT   BINDING         64
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: H
FT   BINDING         77
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         87
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT   Group: 1; Condition: C
FT   From: PRU00004
XX
Size: 200-450;
Related: None;
Template: P03695;
Scope:
 Viruses
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: None
Comments: None
XX
# Revision 1.5 2022/11/19
//