ID A0A172JGK0_9CAUD Unreviewed; 565 AA.
AC A0A172JGK0;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=DNA helicase/primase {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04154};
GN ORFNames=sh5_0022 {ECO:0000313|EMBL:AMR59639.1};
OS Citrobacter phage SH5.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Studiervirinae; Kayfunavirus; Kayfunavirus SH4.
OX NCBI_TaxID=1805468 {ECO:0000313|EMBL:AMR59639.1, ECO:0000313|Proteomes:UP000222579};
RN [1] {ECO:0000313|EMBL:AMR59639.1, ECO:0000313|Proteomes:UP000222579}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hamdi S., Rousseau G.M., Labrie S.J., Saied Kourda R., Tremblay D.M.,
RA Moineau S., Ben Slama K.;
RT "Characterization of five Podoviridae phages infecting Citrobacter
RT freundii.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral
CC DNA replication and recombination. The helicase moves 5' -> 3' on the
CC lagging strand template, unwinding the DNA duplex ahead of the leading
CC strand polymerase at the replication fork and generating ssDNA for both
CC leading and lagging strand synthesis. ATP or dTTP hydrolysis propels
CC each helicase domain to translocate sequentially along DNA. Mediates
CC strand transfer when a joint molecule is available and participates in
CC recombinational DNA repair through its role in strand exchange. Primase
CC activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the
CC lagging strand that the polymerase elongates using dNTPs and providing
CC the primase is still present. {ECO:0000256|HAMAP-Rule:MF_04154}.
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; EC=3.6.4.12;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000256|HAMAP-
CC Rule:MF_04154};
CC -!- SUBUNIT: Homohexamer. Assembles as a hexamer onto linear or circular
CC ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with
CC the viral DNA polymerase that is bound to DNA; this interaction is
CC essential to initiate leading-strand DNA synthesis. The priming complex
CC consists of 2 DNA polymerases and 1 helicase-primase hexamer that
CC assemble on the DNA template. Interacts with the single-stranded DNA-
CC binding protein. Part of the replicase complex that includes the DNA
CC polymerase, the primase/helicase and the single-stranded DNA binding
CC protein. {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- DOMAIN: The N-terminus zinc finger domain is essential for delivering
CC the primed DNA template to the DNA polymerase. The central core domain
CC contains the primase activity. The C-terminus region is responsible for
CC the helicase activity and binds 1 Mg(2+)-dTTP. {ECO:0000256|HAMAP-
CC Rule:MF_04154}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04154}.
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DR EMBL; KU687351; AMR59639.1; -; Genomic_DNA.
DR Proteomes; UP000222579; Genome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR CDD; cd19483; RecA-like_Gp4D_helicase; 1.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.20.25.180; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04154; Helic_Prim_T7; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR048774; Helic-prim_T7_N.
DR InterPro; IPR046394; Helic_Prim_T7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; T7-LIKE MITOCHONDRIAL DNA HELICASE; 1.
DR PANTHER; PTHR12873:SF0; TWINKLE MTDNA HELICASE; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF21268; Helic-prim_T7_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR SMART; SM00382; AAA; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04154, ECO:0000313|EMBL:AMR59639.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04154};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04154}.
FT DOMAIN 282..549
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT ZN_FING 17..39
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 238
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 313..320
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 361
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 466
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 505
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 523
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 536
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 565 AA; 62239 MW; 67F9C7CDB3166629 CRC64;
MVSSEEEDSV FLYHAPCPDC GSSDAMGVFS DGHCYCYACD PSVAWKKGDM ELTEGYTPSG
GKKQVSNLLT WGENSGRYVP LPARGLSADI CKKYSYWVGM MQGKMVQIAD YYDRSGTKVG
QKVRDADKNF TAIGSVKNDL LFGSQLWSGG KKIVITEGEI DCLSVAQVQE GKYPVVSLPL
GAKSAKKTLA ANLEYLDQFE EIILMFDMDE PGREAVEQGA PVLPAGKVKV AFINGYKDAN
AALQAKDFRA IQDAIWNAKP FVPAGVVSAK SLKDRTREAM LKAETEGLLF SSCTTLNAMT
LGARSGELIM VTSGSGMGKS TFVRQLLLEW GRQGKRVGMA MLEEAVEETV QDLIGLDNNV
RLRQSKELKE AILQDGRFDE WYDKLFNDDK FHLYDSFAES EEDTLFAKLG YMVDGLDCDV
ILLDHISIVV SGMEDNSDER KTIDRIMTRL KKFAKTKGVV VVVICHLKNP EKGKSHEEGR
PVSITDLRGS GALRQLSDTI IALERNQQGD TPNVVQLRLL KCRFTGDTGI AGHLEYNKLT
GWLEPTVQTG GSGEEDSSSW ENNDF
//
