SSB_BPT2
ID SSB_BPT2 Reviewed; 302 AA.
AC P09035; Q7Y4N4;
DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT 07-APR-2021, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000255|HAMAP-Rule:MF_04152};
DE Short=SSB protein {ECO:0000255|HAMAP-Rule:MF_04152};
DE AltName: Full=Gp32 {ECO:0000255|HAMAP-Rule:MF_04152};
DE AltName: Full=Helix-destabilizing protein {ECO:0000255|HAMAP-Rule:MF_04152};
GN Name=32 {ECO:0000255|HAMAP-Rule:MF_04152}; Synonyms=ssb;
GN ORFNames=EcT2_00246 {ECO:0000312|EMBL:BBF63397.1};
OS Enterobacteria phage T2 (Bacteriophage T2).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Myoviridae; Tevenvirinae; Tequatrovirus.
OX NCBI_TaxID=10664;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=3262868; DOI=10.1093/nar/16.19.9341;
RA McPheeters D.S., Stormo G.D., Gosch G., Gold L.;
RT "Nucleotide sequences of the bacteriophage T2 and T6 gene 32 mRNAs.";
RL Nucleic Acids Res. 16:9341-9341(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T2L;
RX PubMed=14596796; DOI=10.1016/j.jmb.2003.09.027;
RA Liu Q., Belle A., Shub D.A., Belfort M., Edgell D.R.;
RT "SegG endonuclease promotes marker exclusion and mediates co-conversion
RT from a distant cleavage site.";
RL J. Mol. Biol. 334:13-23(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Akiyama T., Ando H., Kitao T., Shimada K.;
RT "Complete genome sequence of bacteriophage T2.";
RL Submitted (JUL-2018) 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:0000255|HAMAP-Rule:MF_04152}.
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:0000255|HAMAP-Rule:MF_04152}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_04152}.
CC -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding
CC protein family. {ECO:0000255|HAMAP-Rule:MF_04152}.
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DR EMBL; X12460; CAA31000.1; -; mRNA.
DR EMBL; X12460; CAA31001.1; ALT_SEQ; mRNA.
DR EMBL; AY310907; AAP78913.1; -; Genomic_DNA.
DR EMBL; AP018813; BBF63397.1; -; Genomic_DNA.
DR PIR; S01437; DDBP32.
DR SMR; P09035; -.
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: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 HAMAP; MF_04152; SSB_T4; 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 InterPro; IPR046395; SSB_T4.
DR Pfam; PF08804; gp32; 1.
DR SUPFAM; SSF50249; SSF50249; 1.
PE 2: Evidence at transcript level;
KW DNA damage; DNA repair; DNA replication; DNA-binding; Metal-binding;
KW Repressor; Viral DNA replication; Zinc.
FT CHAIN 1..302
FT /note="Single-stranded DNA-binding protein"
FT /id="PRO_0000165048"
FT REGION 3..7
FT /note="LAST"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152"
FT REGION 273..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..293
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 65
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152"
FT BINDING 88
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04152"
SQ SEQUENCE 302 AA; 33478 MW; C74A3052E36A0C94 CRC64;
MFKRKSTAEL AAQMAKLAGN KGGFSSEDKG EWKLKLDNAG NGQAVIRFLP SKNDEQAPFA
ILVNHGFKKN GKWYIENCSS THGDYDSCPV CQYISKNDLY NTDNKEYGLV KRKTSYWANI
LVVKDPAAPE NEGKVFKYRF GKKIWDKINA MIAVDVEMGE TPVDVTCPWE GANFVLKVKQ
VSGFSNYDES KFLNQSAIPN IDDESFQKEL FEQMVDLSEM TSKDKFKSFE ELSTKFSQVM
GTAAMGGAAA TAAKKADKVA DDLDAFNVDD FNTKTEDDFM SSSSGSSSSA DDTDLDDLLN
DL
