ID A0A159B7D6_9CAUD Unreviewed; 302 AA. AC A0A159B7D6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 14-DEC-2022, entry version 23. DE RecName: Full=Single-stranded DNA-binding protein {ECO:0000256|ARBA:ARBA00018590, ECO:0000256|HAMAP-Rule:MF_04152}; DE Short=SSB protein {ECO:0000256|HAMAP-Rule:MF_04152}; DE AltName: Full=Gp32 {ECO:0000256|ARBA:ARBA00031936, ECO:0000256|HAMAP-Rule:MF_04152}; DE AltName: Full=Helix-destabilizing protein {ECO:0000256|ARBA:ARBA00032941, ECO:0000256|HAMAP-Rule:MF_04152}; GN Name=32 {ECO:0000256|HAMAP-Rule:MF_04152}; GN Synonyms=ssb {ECO:0000256|HAMAP-Rule:MF_04152}; GN ORFNames=HY03_0245 {ECO:0000313|EMBL:AKJ72887.1}; OS Escherichia phage HY03. OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes; OC Straboviridae; Tevenvirinae; Tequatrovirus; Tequatrovirus hy03. OX NCBI_TaxID=1654926 {ECO:0000313|EMBL:AKJ72887.1, ECO:0000313|Proteomes:UP000204314}; RN [1] {ECO:0000313|EMBL:AKJ72887.1, ECO:0000313|Proteomes:UP000204314} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Lee J.-H., Park E.-A., Lee D.-H.; RT "Complete Genome Sequence of E. coli O157:H7 Bacteriophage HY03."; RL Submitted (APR-2015) 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:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_04152}. CC -!- SIMILARITY: Belongs to the Tequatrovirus single-stranded DNA-binding CC protein family. {ECO:0000256|HAMAP-Rule:MF_04152}. 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; KR269718; AKJ72887.1; -; Genomic_DNA. DR RefSeq; YP_009284218.1; NC_031047.1. DR GeneID; 29079086; -. DR KEGG; vg:29079086; -. DR Proteomes; UP000204314; Genome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0039686; P:bidirectional double-stranded viral DNA replication; IEA:UniProtKB-UniRule. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. 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; Nucleic acid-binding proteins; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_04152}; KW DNA recombination {ECO:0000256|HAMAP-Rule:MF_04152}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_04152}; KW DNA replication {ECO:0000256|ARBA:ARBA00023109, ECO:0000256|HAMAP- KW Rule:MF_04152}; KW DNA-binding {ECO:0000256|HAMAP-Rule:MF_04152, ECO:0000313|EMBL:AKJ72887.1}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04152}; KW Repressor {ECO:0000256|ARBA:ARBA00022491, ECO:0000256|HAMAP-Rule:MF_04152}; KW Viral DNA replication {ECO:0000256|ARBA:ARBA00023109, ECO:0000256|HAMAP- KW Rule:MF_04152}; Zinc {ECO:0000256|HAMAP-Rule:MF_04152}. FT DOMAIN 40..240 FT /note="gp32" FT /evidence="ECO:0000259|Pfam:PF08804" FT REGION 3..7 FT /note="LAST" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04152" FT REGION 275..302 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 278..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:0000256|HAMAP-Rule:MF_04152" FT BINDING 78 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04152" FT BINDING 88 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04152" FT BINDING 91 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_04152" SQ SEQUENCE 302 AA; 33509 MW; 53AC1C17C8921788 CRC64; MFKRKSTAEL AAQMAKLAGN KGGFSSEDKG EWKLKLDNAG NGQAVIRFLP SKNDEQAPFA ILVNHGFKKN GKWYIETCSS THGDYDSCPV CQYISKNDLY NTDNKEYSLV KRKTSYWANI LVVKDPAAPE NEGKVFKYRF GKKIWDKINA MIAVDVEMGE TPVDVTCPWE GANFVLKVKQ VSGFSNYDES KFLNQSAIPN IDDESFQKEL FEQMVDLSEM TSKDKFKSFE ELSTKFSQVM GTAAMGGAAA TAAKKADKVA DDLDAFNVDD FKTKTEDDFM SSSSGSSSSA DDTDLDDLLN DL //