ID PRIM_BPP4 Reviewed; 777 AA.
AC P10277;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 24-JAN-2024, entry version 146.
DE RecName: Full=Putative P4-specific DNA primase;
DE EC=2.7.7.-;
DE EC=3.6.4.12;
GN Name=Alpha;
OS Enterobacteria phage P4 (Bacteriophage P4).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=10680;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3309336; DOI=10.1016/0022-2836(87)90664-4;
RA Flensburg J., Calendar R.;
RT "Bacteriophage P4 DNA replication. Nucleotide sequence of the P4
RT replication gene and the cis replication region.";
RL J. Mol. Biol. 195:439-445(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2183201; DOI=10.1093/nar/18.6.1649;
RA Halling C., Calendar R., Christie G.E., Dale E.C., Deho G., Finkel S.,
RA Flensburg J., Ghisotti D., Kahn M.L., Lane K.B., Lin C.-S., Lindqvist B.H.,
RA Pierson L.S., Six E.W., Sunshine M.G., Ziermann R.;
RT "DNA sequence of satellite bacteriophage P4.";
RL Nucleic Acids Res. 18:1649-1649(1990).
RN [3]
RP CHARACTERIZATION.
RX PubMed=8253092; DOI=10.1002/j.1460-2075.1993.tb06045.x;
RA Ziegelin G., Scherzinger E., Lurz R., Lanka E.;
RT "Phage P4 alpha protein is multifunctional with origin recognition,
RT helicase and primase activities.";
RL EMBO J. 12:3703-3708(1993).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 671-770.
RX PubMed=11929537; DOI=10.1046/j.1365-2958.2002.02796.x;
RA Yeo H.J., Ziegelin G., Korolev S., Calendar R., Lanka E., Waksman G.;
RT "Phage P4 origin-binding domain structure reveals a mechanism for
RT regulation of DNA-binding activity by homo- and heterodimerization of
RT winged helix proteins.";
RL Mol. Microbiol. 43:855-867(2002).
CC -!- FUNCTION: This protein acts as a DNA primase generating di- to
CC pentaribonucleotides; the predominant product being the dimer pppApG.
CC It complexes specifically to the P4 origin of replication (ori) and its
CC cis replication region (crr). It also acts as a DNA helicase.
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 -!- SUBUNIT: Homohexamer.
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DR EMBL; X05623; CAA29111.1; -; Genomic_DNA.
DR EMBL; X51522; CAA35898.1; -; Genomic_DNA.
DR RefSeq; NP_042036.1; NC_001609.1.
DR PDB; 1KA8; X-ray; 2.95 A; A/B/C/D/E/F=671-770.
DR PDBsum; 1KA8; -.
DR SMR; P10277; -.
DR GeneID; 1261095; -.
DR KEGG; vg:1261095; -.
DR OrthoDB; 3810at10239; -.
DR EvolutionaryTrace; P10277; -.
DR Proteomes; UP000009093; Genome.
DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003896; F:DNA primase activity; IDA:CACAO.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR Gene3D; 3.90.580.10; Zinc finger, CHC2-type domain; 1.
DR InterPro; IPR004968; DNA_primase/NTPase_C.
DR InterPro; IPR036977; DNA_primase_Znf_CHC2.
DR InterPro; IPR014015; Helicase_SF3_DNA-vir.
DR InterPro; IPR045455; NrS-1_pol-like_helicase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR014818; Phage/plasmid_primase_P4_C.
DR InterPro; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR PANTHER; PTHR35372; ATP BINDING PROTEIN-RELATED; 1.
DR PANTHER; PTHR35372:SF2; SF3 HELICASE DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF08706; D5_N; 1.
DR Pfam; PF19263; DUF5906; 1.
DR Pfam; PF03288; Pox_D5; 1.
DR Pfam; PF08273; Prim_Zn_Ribbon; 1.
DR Pfam; PF13362; Toprim_3; 1.
DR SMART; SM00885; D5_N; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51206; SF3_HELICASE_1; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA replication; DNA-binding;
KW DNA-directed RNA polymerase; Helicase; Hydrolase; Metal-binding;
KW Nucleotide-binding; Nucleotidyltransferase; Primosome; Reference proteome;
KW Transcription; Transferase; Zinc; Zinc-finger.
FT CHAIN 1..777
FT /note="Putative P4-specific DNA primase"
FT /id="PRO_0000165224"
FT DOMAIN 208..296
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT DOMAIN 474..627
FT /note="SF3 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT ZN_FING 35..60
FT /note="CHC2-type"
FT /evidence="ECO:0000305"
FT BINDING 501..508
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00551"
FT HELIX 674..678
FT /evidence="ECO:0007829|PDB:1KA8"
FT HELIX 679..681
FT /evidence="ECO:0007829|PDB:1KA8"
FT STRAND 682..684
FT /evidence="ECO:0007829|PDB:1KA8"
FT STRAND 686..688
FT /evidence="ECO:0007829|PDB:1KA8"
FT TURN 703..705
FT /evidence="ECO:0007829|PDB:1KA8"
FT HELIX 707..717
FT /evidence="ECO:0007829|PDB:1KA8"
FT HELIX 726..739
FT /evidence="ECO:0007829|PDB:1KA8"
FT STRAND 746..749
FT /evidence="ECO:0007829|PDB:1KA8"
FT STRAND 752..759
FT /evidence="ECO:0007829|PDB:1KA8"
FT HELIX 762..766
FT /evidence="ECO:0007829|PDB:1KA8"
SQ SEQUENCE 777 AA; 84919 MW; E86B57991FAE46B0 CRC64;
MKMNVTATVS HALGHWPRIL PALGIQVLKN RHQPCPVCGG SDRFRFDDRE GRGTWYCNQC
GAGDGLKLVE KVFGVSPSDA AAKVAAVTGS LPPADPAVTT AAVDETDAAR KNAAALAQTL
MAKTRTGTGN AYLTRKGFPG RECRMLTGTH RAGGVSWRAG DLVVPLYDDS GELVNLQLIS
ADGRKRTLKG GQVRGTCHTL EGQNQAGKRL WIAEGYATAL TVHHLTGETV MVALSSVNLL
SLASLARQKH PACQIVLAAD RDLSGDGQKK AAAAADACEG VVALPPVFGD WNDAFTQYGG
EATRKAIYDA IRPPAESPFD TMSEAEFSAM STSEKAMRIY EHYGEALAVD ANGQLLSRYE
NGVWKVLPPQ DFARDVAGLF QRLRAPFSSG KVASVVDTLK LIIPQQEAPS RRLIGFRNGV
LDTQNGTFHP HSPSHWMRTL CDVDFTPPVD GETLETHAPA FWRWLDRAAG GRAEKRDVIL
AALFMVLANR YDWQLFLEVT GPGGSGKSIM AEIATLLAGE DNATSATIET LESPRERAAL
TGFSLIRLPD QEKWSGDGAG LKAITGGDAV SVDPKYRDAY STHIPAVILA VNNNPMRFTD
RSGGVSRRRV IIHFPEQIAP QERDPQLKDK ITRELAVIVR HLMQKFSDPM LARSLLQSQQ
NSDEALNIKR DADPTFDFIG YLETLPQTSG MYMGNASIIP RNYRKYLYHA YLAYMEANGY
RNVLSLKMFG LGLPVMLKEY GLNYEKRHTK QGIQTNLTLK EESYGDWLPK CDDPTTA
//
