VG12_BPP22
ID VG12_BPP22 Reviewed; 458 AA.
AC P03006; Q7PCE7;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
DE AltName: Full=Replication protein gp12;
GN Name=12;
OS Salmonella phage P22 (Bacteriophage P22).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Podoviridae; Lederbergvirus.
OX NCBI_TaxID=10754;
OH NCBI_TaxID=90371; Salmonella typhimurium.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6241581; DOI=10.1016/0378-1119(84)90004-0;
RA Backhaus H., Petri J.B.;
RT "Sequence analysis of a region from the early right operon in phage P22
RT including the replication genes 18 and 12.";
RL Gene 32:289-303(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11053393; DOI=10.1128/jb.182.22.6472-6481.2000;
RA Vander Byl C.S., Kropinski A.M.B.;
RT "Sequence of the genome of Salmonella bacteriophage P22.";
RL J. Bacteriol. 182:6472-6481(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12562822; DOI=10.1128/jb.185.4.1475-1477.2003;
RA Pedulla M.L., Ford M.E., Karthikeyan T., Houtz J.M., Hendrix R.W.,
RA Hatfull G.F., Poteete A.R., Gilcrease E.B., Winn-Stapley D.A.,
RA Casjens S.R.;
RT "Corrected sequence of the bacteriophage P22 genome.";
RL J. Bacteriol. 185:1475-1477(2003).
CC -!- FUNCTION: Renders P22 DNA replication independent of a functional dnaB
CC gene of the host.
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 -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; X78401; CAA55156.1; -; Genomic_DNA.
DR EMBL; M10074; AAA32276.1; -; Genomic_DNA.
DR EMBL; AF217253; AAF75029.1; -; Genomic_DNA.
DR EMBL; BK000583; DAA01026.1; -; Genomic_DNA.
DR PIR; A03536; Z2BPC2.
DR RefSeq; NP_059611.1; NC_002371.2.
DR SMR; P03006; -.
DR GeneID; 1262823; -.
DR KEGG; vg:1262823; -.
DR Proteomes; UP000001795; Genome.
DR Proteomes; UP000007960; Genome.
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:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR007693; DNA_helicase_DnaB-like_N.
DR InterPro; IPR016136; DNA_helicase_N/primase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Early protein; Helicase;
KW Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..458
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102015"
FT DOMAIN 164..436
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT REGION 355..375
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 195..202
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 50127 MW; 7981F1C2A5293322 CRC64;
MRQDIEASVI GGLLIGGLTP TASDVLATLE PEAFSIPLYR KAFEVIRKQA RNRNLIDGLM
VAEECGDEYA TAVMMTARSC PSAANLKGYA GMVADSYQRR QVLQLLDEMR EPISNGTLDA
SGRAMDELVK RLSSIRKPRN EVKPVRLGEI INDYTDTLDR RLRNGEESDT LKTGIEELDA
ITGGMNAEDL VIIAARPGMG KTELALKIAE GVASRVIPGS GVRRGVLIFS MEMSAIQVVE
RGIAGAGMMS VSVLRNPSRM DDEGWARVAS GMKLLAELDV WVVDASRLSV EEIRSISERH
KQEHPNLSLI MADYLGLIEK PKAERNDLAI AHISGSLKAM AKDLKTPVIS LSQLSRDVEK
RPNKRPTNAD LRDSGSIEQD ADSIIMLYRE AVYDENSSAA PFAEIIVTKN RFGSLGTVYQ
RFCNGHFVAC DQDEARQICT ASNAPAGRRK RYAQGADV