ID   OBP_BPT5                Reviewed;         928 AA.
AC   Q6QGH9; Q66LV7;
DT   17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Putative replication origin binding protein;
DE   AltName: Full=D2 helicase {ECO:0000303|PubMed:23435232};
GN   Name=obp {ECO:0000312|EMBL:AAX12037.1}; Synonyms=D2;
GN   ORFNames=T5.108 {ECO:0000312|EMBL:AAS77154.1},
GN   T5p106 {ECO:0000312|EMBL:AAU05245.1};
OS   Escherichia phage T5 (Enterobacteria phage T5).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Demerecviridae; Markadamsvirinae; Tequintavirus.
OX   NCBI_TaxID=2695836;
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Ksenzenko V.N., Kaliman A.V., Krutilina A.I., Shlyapnikov M.G.;
RT   "Bacteriophage T5 complete genome.";
RL   Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 11303-B5;
RX   PubMed=15661140; DOI=10.1016/j.virol.2004.10.049;
RA   Wang J., Jiang Y., Vincent M., Sun Y., Yu H., Wang J., Bao Q., Kong H.,
RA   Hu S.;
RT   "Complete genome sequence of bacteriophage T5.";
RL   Virology 332:45-65(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St0 deletion mutant;
RX   PubMed=24198424; DOI=10.1128/jvi.02262-13;
RA   Zivanovic Y., Confalonieri F., Ponchon L., Lurz R., Chami M., Flayhan A.,
RA   Renouard M., Huet A., Decottignies P., Davidson A.R., Breyton C.,
RA   Boulanger P.;
RT   "Insights into bacteriophage T5 structure from analysis of its
RT   morphogenesis genes and protein components.";
RL   J. Virol. 88:1162-1174(2014).
RN   [4]
RP   FUNCTION, AND MUTAGENESIS OF LYS-405.
RX   PubMed=23435232; DOI=10.1093/nar/gkt105;
RA   Wong I.N., Sayers J.R., Sanders C.M.;
RT   "Characterization of an unusual bipolar helicase encoded by bacteriophage
RT   T5.";
RL   Nucleic Acids Res. 41:4587-4600(2013).
CC   -!- FUNCTION: Displays bipolar ssDNA and dsDNA unwinding activities that
CC       require the same core catalytic residues for unwinding in either
CC       direction, the 3'-5' direction being more robust.
CC       {ECO:0000269|PubMed:23435232}.
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000305|PubMed:15661140}.
CC   -!- SIMILARITY: Belongs to the herpesviridae oribp family. {ECO:0000305}.
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DR   EMBL; AY543070; AAS77154.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12037.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05245.1; -; Genomic_DNA.
DR   RefSeq; YP_006936.1; NC_005859.1.
DR   GeneID; 2777687; -.
DR   KEGG; vg:2777687; -.
DR   Proteomes; UP000002107; Genome.
DR   Proteomes; UP000002141; Genome.
DR   Proteomes; UP000002503; Genome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IDA:GO_Central.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR003450; Replication_origin-bd.
DR   Pfam; PF02399; Herpes_ori_bp; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; DNA-binding; Early protein; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..928
FT                   /note="Putative replication origin binding protein"
FT                   /id="PRO_0000435554"
FT   DOMAIN          386..516
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           484..487
FT                   /note="DEAD box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         399..406
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MUTAGEN         405
FT                   /note="K->E: Complete loss of ATPase and helicase
FT                   activities. No effect on ssDNA binding."
FT                   /evidence="ECO:0000269|PubMed:23435232"
FT   CONFLICT        262
FT                   /note="E -> G (in Ref. 3; AAU05245)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   928 AA;  105350 MW;  50F72DE4A038FC98 CRC64;
     MFSILQGHAG FSRDLATGIW REIKAEDYTF AKRFSKEHPE GKPASMPFKF DVIEEHDPQS
     LAEMLPLMRR LTSDPHIVAV RGRCLAPKNN VRRKKGNFNV SNPSNIIAMD VDGILDTGGY
     DKFNLVGMAR HIIKMLNSIS EDMFPLDAGF IAHASSSAGL KPGIRMHLML ESNVKVTQGQ
     LKFLFTSIND SSKQKFGFDI ADLAYYSSVQ LHYFADPLFS DGIVDPFKAE SKPRLVYVKG
     SKVNLPNNLV DYETTRGEFK EEFYSLLDQI KGKKIASDKV EETISELEEA DDGVYLRIIP
     KLYHRALEDG VDFAWLEREI KPALSEYIAT KDNSRNIQDY FNNGRKQALK AFVNNSKREI
     PLNLKGVPLK KLEVDSPPEV PYLKINIVPP KGHITFVKAS LGTGKTTAVT KWLDAGVLPG
     NFLAVTNTRA LVSSNAKKFS AGQYDKSVDM LNFKRGAIDR MSTTIHSLHK FKSFIGQIDT
     IFIDECDAVM NDLLFAPVVK QRRECIQVLR DILMTAKTVI LSDGDISAET IEAYGSLIDF
     DKPVAFYNHH RKMLSKAHAY EFPDESSIWV ALQTSLEMGE KSILVSDCGP DELNEKGMAL
     RRNTGALVKE IHSNSTSDVD IRRILDYTTN ELIDQQIDCL LCSPSVTSGV DFNYFDNVFV
     ITRTSNQAPN MRFQAIRRDR GAQNIYYFID KSTSGFSAGS EQYNIDEGWL ELAQQLYARR
     RELESRNYTS TLRYYLLDQG ATIDIFSESW GTIEGAGKEY TEERIKAILH STPDYCAPRH
     ADAYEAKLLL VRYYHLESIK DVTVEHVEQY IKDKPNDRAA FFHKMHEMFW EDIKKCSNVT
     IKPFIEALKG KKKDFFLKTG QSANPKYARM YLGMMGIGKD MNTENIVDWY RTYCKIECMP
     IPFKFMTEEE RAMAEEVMSE LGATNEDA