ID   HEL10_BPT5              Reviewed;         450 AA.
AC   P11107; Q5DMH9; Q66LU1;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1989, sequence version 1.
DT   03-AUG-2022, entry version 99.
DE   RecName: Full=Probable helicase D10 {ECO:0000312|EMBL:AAX12052.1};
DE            EC=3.6.4.-;
DE   AltName: Full=Protein D10;
GN   Name=D10;
GN   ORFNames=T5.124 {ECO:0000312|EMBL:AAS77170.1},
GN   T5p122 {ECO:0000312|EMBL:AAU05261.1};
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 [GENOMIC DNA], AND INDUCTION.
RX   PubMed=3057441; DOI=10.1093/nar/16.21.10353;
RA   Kaliman A.V., Kryukov V.M., Bayev A.A.;
RT   "The nucleotide sequence of the region of bacteriophage T5 early genes D10-
RT   D15.";
RL   Nucleic Acids Res. 16:10353-10354(1988).
RN   [2]
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND INDUCTION.
RC   STRAIN=ATCC 11303-B5 {ECO:0000312|EMBL:AAX12052.1};
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   [4]
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   [5]
RP   PROBABLE FUNCTION.
RX   PubMed=2547651; DOI=10.1016/0014-5793(89)80887-7;
RA   Blinov V.M., Koonin E.V., Gorbalenya A.E., Kaliman A.V., Kryukov V.M.;
RT   "Two early genes of bacteriophage T5 encode proteins containing an NTP-
RT   binding sequence motif and probably involved in DNA replication,
RT   recombination and repair.";
RL   FEBS Lett. 252:47-52(1989).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC   -!- INDUCTION: Expressed in the early phase of the viral replicative cycle.
CC       {ECO:0000269|PubMed:3057441, ECO:0000305|PubMed:15661140}.
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DR   EMBL; AY543070; AAS77170.1; -; Genomic_DNA.
DR   EMBL; AY692264; AAU05261.1; -; Genomic_DNA.
DR   EMBL; AY587007; AAX12052.1; -; Genomic_DNA.
DR   PIR; S01931; WABPT5.
DR   RefSeq; YP_006952.1; NC_005859.1.
DR   SMR; P11107; -.
DR   PRIDE; P11107; -.
DR   GeneID; 2777605; -.
DR   KEGG; vg:2777605; -.
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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IMP:CACAO.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009378; F:four-way junction helicase activity; IDA:CACAO.
DR   GO; GO:0032508; P:DNA duplex unwinding; IDA:CACAO.
DR   Gene3D; 3.40.50.300; -; 2.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF00271; Helicase_C; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; DNA-binding; Early protein; Helicase; Hydrolase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..450
FT                   /note="Probable helicase D10"
FT                   /id="PRO_0000165214"
FT   DOMAIN          95..240
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          289..439
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT   MOTIF           193..196
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   BINDING         108..115
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT   CONFLICT        318
FT                   /note="L -> F (in Ref. 4; AAU05261)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   450 AA;  50365 MW;  54FBD63958EBBB93 CRC64;
     MKVVISNKAY FKPDDELWDY CSKQTTYHIE TMTSKYPIMY KNSGVVAKEI KWIPITRLDL
     LDAKGIKYEL VDKRTLAPVD IPKPKFKLRE EDQLPIYEEC DDTCIINGKP GFGKTILALA
     LAYKFGQKTL VICTNTSIRE MWAAEVRKWF GFEPGIIGSG KYNIDPPIVV SNIQTVNKHA
     NNLSKVFGTV IVDEVHHCVA TTFTNFLEIS CARYKIGLSG TLKRKDGLQV MFKDFFGYKI
     FSPPVNNTVA PTIHRYSVPV ELSGNQNVPW ALRANDVYNH PEYRETIINL AHLYVNMGHK
     VLIVSDRTEL IQTILEALTQ RGVTTYEIIG ATHLDDRLKI QEDIAKGGPC VLAAAQSIFS
     EGISLNELSC LIMGSLINNE SLIEQLAGRV QRIVEGKLDP IVVDLIMKGG TGLRQASGRM
     AVYRNNGWKT ITMTPEKAVQ LAKIAFGNSS