SSB_BPT7
ID SSB_BPT7 Reviewed; 232 AA.
AC P03696;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=2.5 protein {ECO:0000255|HAMAP-Rule:MF_04153};
DE AltName: Full=Gene product 2.5 {ECO:0000255|HAMAP-Rule:MF_04153};
DE Short=gp2.5 {ECO:0000255|HAMAP-Rule:MF_04153};
GN OrderedLocusNames=2.5;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA Dunn J.J., Studier F.W.;
RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT the beginning of gene 4.";
RL J. Mol. Biol. 148:303-330(1981).
RN [3]
RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF PHE-232.
RX PubMed=1634538; DOI=10.1016/s0021-9258(18)42141-2;
RA Kim Y.T., Tabor S., Bortner C., Grifith J.D., Richardson C.C.;
RT "Purification and characterization of the bacteriophage T7 gene 2.5
RT protein. A single-stranded DNA-binding protein.";
RL J. Biol. Chem. 267:15022-15031(1992).
RN [4]
RP INTERACTION WITH THE VIRAL HELICASE AND DNA POLYMERASE.
RX PubMed=1634539; DOI=10.1016/s0021-9258(18)42142-4;
RA Kim Y.T., Tabor S., Churchich J.E., Richardson C.C.;
RT "Interactions of gene 2.5 protein and DNA polymerase of bacteriophage T7.";
RL J. Biol. Chem. 267:15032-15040(1992).
RN [5]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE, AND DOMAIN.
RX PubMed=8106511; DOI=10.1016/s0021-9258(17)37684-6;
RA Kim Y.T., Richardson C.C.;
RT "Acidic carboxyl-terminal domain of gene 2.5 protein of bacteriophage T7 is
RT essential for protein-protein interactions.";
RL J. Biol. Chem. 269:5270-5278(1994).
RN [6]
RP FUNCTION.
RX PubMed=8617248; DOI=10.1002/j.1460-2075.1996.tb00552.x;
RA Kong D., Richardson C.C.;
RT "Single-stranded DNA binding protein and DNA helicase of bacteriophage T7
RT mediate homologous DNA strand exchange.";
RL EMBO J. 15:2010-2019(1996).
RN [7]
RP FUNCTION.
RX PubMed=9079662; DOI=10.1074/jbc.272.13.8380;
RA Kong D., Nossal N.G., Richardson C.C.;
RT "Role of the bacteriophage T7 and T4 single-stranded DNA-binding proteins
RT in the formation of joint molecules and DNA helicase-catalyzed polar branch
RT migration.";
RL J. Biol. Chem. 272:8380-8387(1997).
RN [8]
RP FUNCTION.
RX PubMed=9651583; DOI=10.1016/s1097-2765(00)80100-8;
RA Lee J., Chastain P.D. II, Kusakabe T., Griffith J.D., Richardson C.C.;
RT "Coordinated leading and lagging strand DNA synthesis on a minicircular
RT template.";
RL Mol. Cell 1:1001-1010(1998).
RN [9]
RP FUNCTION.
RX PubMed=11222583; DOI=10.1128/jb.183.6.1862-1869.2001;
RA Yu M., Masker W.;
RT "T7 single strand DNA binding protein but not T7 helicase is required for
RT DNA double strand break repair.";
RL J. Bacteriol. 183:1862-1869(2001).
RN [10]
RP DOMAIN, MUTAGENESIS OF PHE-232, AND INTERACTION WITH THE VIRAL DNA
RP POLYMERASE.
RX PubMed=12766155; DOI=10.1074/jbc.m304318200;
RA He Z.G., Rezende L.F., Willcox S., Griffith J.D., Richardson C.C.;
RT "The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-
RT binding protein modulates DNA binding and interaction with T7 DNA
RT polymerase.";
RL J. Biol. Chem. 278:29538-29545(2003).
RN [11]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=15795374; DOI=10.1073/pnas.0501637102;
RA Hamdan S.M., Marintcheva B., Cook T., Lee S.J., Tabor S., Richardson C.C.;
RT "A unique loop in T7 DNA polymerase mediates the binding of helicase-
RT primase, DNA binding protein, and processivity factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5096-5101(2005).
RN [12]
RP FUNCTION, AND DOMAIN.
RX PubMed=16807232; DOI=10.1074/jbc.m604601200;
RA Marintcheva B., Hamdan S.M., Lee S.J., Richardson C.C.;
RT "Essential residues in the C terminus of the bacteriophage T7 gene 2.5
RT single-stranded DNA-binding protein.";
RL J. Biol. Chem. 281:25831-25840(2006).
RN [13]
RP IDENTIFICATION IN THE REPLICASE COMPLEX.
RX PubMed=22977246; DOI=10.1074/jbc.m112.410647;
RA Kulczyk A.W., Akabayov B., Lee S.J., Bostina M., Berkowitz S.A.,
RA Richardson C.C.;
RT "An interaction between DNA polymerase and helicase is essential for the
RT high processivity of the bacteriophage T7 replisome.";
RL J. Biol. Chem. 287:39050-39060(2012).
RN [14]
RP REVIEW.
RX PubMed=29588157; DOI=10.1016/j.semcdb.2018.03.018;
RA Hernandez A.J., Richardson C.C.;
RT "Gp2.5, the multifunctional bacteriophage T7 single-stranded DNA binding
RT protein.";
RL Semin. Cell Dev. Biol. 86:92-101(2019).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-206, AND SUBUNIT.
RX PubMed=11481454; DOI=10.1073/pnas.171317698;
RA Hollis T., Stattel J.M., Walther D.S., Richardson C.C., Ellenberger T.;
RT "Structure of the gene 2.5 protein, a single-stranded DNA binding protein
RT encoded by bacteriophage T7.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9557-9562(2001).
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 (PubMed:16807232, PubMed:8617248,
CC PubMed:9079662, PubMed:11222583). Coats the lagging-strand ssDNA as the
CC replication fork advances and stimulates the activities of viral DNA
CC polymerase and primase/helicase (PubMed:8617248). Coordinates
CC simultaneous synthesis of leading- and lagging-strands
CC (PubMed:9651583). Together with DNA primase/helicase, promotes pairing
CC of two homologous DNA molecules containing complementary single-
CC stranded regions and mediates homologous DNA strand exchange
CC (PubMed:8617248). Promotes also the formation of joint molecules
CC (PubMed:8617248, PubMed:9079662). Disrupts loops, hairpins and other
CC secondary structures present on ssDNA to reduce and eliminate pausing
CC of viral DNA polymerase at specific sites during elongation
CC (PubMed:1634538). {ECO:0000255|HAMAP-Rule:MF_04153,
CC ECO:0000269|PubMed:11222583, ECO:0000269|PubMed:1634538,
CC ECO:0000269|PubMed:16807232, ECO:0000269|PubMed:8617248,
CC ECO:0000269|PubMed:9079662, ECO:0000269|PubMed:9651583}.
CC -!- SUBUNIT: Homodimer (PubMed:1634538, PubMed:11481454). Interacts (via C-
CC terminus) with the viral DNA polymerase (PubMed:15795374,
CC PubMed:1634539, PubMed:8106511, PubMed:12766155). Interacts with the
CC viral helicase/primase (PubMed:1634539). Part of the replicase complex
CC that includes the DNA polymerase, host thioredoxin, the
CC primase/helicase and the single-stranded DNA binding protein
CC (PubMed:22977246). {ECO:0000255|HAMAP-Rule:MF_04153,
CC ECO:0000269|PubMed:11481454, ECO:0000269|PubMed:12766155,
CC ECO:0000269|PubMed:15795374, ECO:0000269|PubMed:1634538,
CC ECO:0000269|PubMed:1634539, ECO:0000269|PubMed:22977246,
CC ECO:0000269|PubMed:8106511}.
CC -!- DOMAIN: The acidic C-terminus is involved in modulating the ssDNA
CC binding properties (PubMed:16807232, PubMed:12766155, PubMed:8106511).
CC It is also required for dimer formation and for interactions with the
CC viral DNA polymerase and the helicase (PubMed:16807232,
CC PubMed:12766155, PubMed:8106511). {ECO:0000255|HAMAP-Rule:MF_04153,
CC ECO:0000269|PubMed:12766155, ECO:0000269|PubMed:16807232,
CC ECO:0000269|PubMed:8106511}.
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; V01146; CAA24400.1; -; Genomic_DNA.
DR EMBL; V01127; CAA24343.1; -; Genomic_DNA.
DR PIR; F94615; DDBPT7.
DR RefSeq; NP_041970.1; NC_001604.1.
DR PDB; 1JE5; X-ray; 1.90 A; A/B=1-206.
DR PDBsum; 1JE5; -.
DR SMR; P03696; -.
DR IntAct; P03696; 1.
DR MINT; P03696; -.
DR GeneID; 1261080; -.
DR KEGG; vg:1261080; -.
DR EvolutionaryTrace; P03696; -.
DR Proteomes; UP000000840; Genome.
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 1: Evidence at protein level;
KW 3D-structure; DNA damage; DNA repair; DNA replication; DNA-binding;
KW Reference proteome; Viral DNA replication.
FT CHAIN 1..232
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000106483"
FT REGION 189..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..232
FT /note="Dimerization and interaction with the viral DNA
FT polymerase and helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04153,
FT ECO:0000269|PubMed:8106511"
FT COMPBIAS 214..232
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 232
FT /note="F->L: Binds 3-fold more tightly to ssDNA. Promotes
FT strand-displacement DNA synthesis by viral DNA polymerase
FT in the absence of the helicase."
FT /evidence="ECO:0000269|PubMed:12766155,
FT ECO:0000269|PubMed:1634539"
FT STRAND 10..13
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 37..45
FT /evidence="ECO:0007829|PDB:1JE5"
FT HELIX 49..74
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 100..115
FT /evidence="ECO:0007829|PDB:1JE5"
FT TURN 117..119
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:1JE5"
FT STRAND 166..179
FT /evidence="ECO:0007829|PDB:1JE5"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1JE5"
SQ SEQUENCE 232 AA; 25694 MW; 2D2EF0B5FB89F3F4 CRC64;
MAKKIFTSAL GTAEPYAYIA KPDYGNEERG FGNPRGVYKV DLTIPNKDPR CQRMVDEIVK
CHEEAYAAAV EEYEANPPAV ARGKKPLKPY EGDMPFFDNG DGTTTFKFKC YASFQDKKTK
ETKHINLVVV DSKGKKMEDV PIIGGGSKLK VKYSLVPYKW NTAVGASVKL QLESVMLVEL
ATFGGGEDDW ADEVEENGYV ASGSAKASKP RDEESWDEDD EESEEADEDG DF
