ID DNAB_HELPY Reviewed; 488 AA. AC O25916; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 1. DT 27-MAR-2024, entry version 132. DE RecName: Full=Replicative DNA helicase; DE EC=3.6.4.12; GN Name=dnaB; OrderedLocusNames=HP_1362; OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori). OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales; OC Helicobacteraceae; Helicobacter. OX NCBI_TaxID=85962; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700392 / 26695; RX PubMed=9252185; DOI=10.1038/41483; RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G., RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A., RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N., RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A., RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E., RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D., RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S., RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.; RT "The complete genome sequence of the gastric pathogen Helicobacter RT pylori."; RL Nature 388:539-547(1997). CC -!- FUNCTION: Participates in initiation and elongation during chromosome CC replication; it exhibits DNA-dependent ATPase activity and contains CC distinct active sites for ATP binding, DNA binding, and interaction CC with DnaC protein, primase, and other prepriming proteins. CC {ECO:0000250}. 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 -!- INTERACTION: CC O25916; O25916: dnaB; NbExp=6; IntAct=EBI-7529552, EBI-7529552; CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000511; AAD08402.1; -; Genomic_DNA. DR PIR; B64690; B64690. DR RefSeq; NP_208154.1; NC_000915.1. DR RefSeq; WP_000349722.1; NC_018939.1. DR PDB; 3GXV; X-ray; 2.20 A; A/B=1-121, C=101-122, D=98-123. DR PDB; 4A1F; X-ray; 2.50 A; A/B=152-488. DR PDB; 4ZC0; X-ray; 6.70 A; A/B/C/D=1-488. DR PDBsum; 3GXV; -. DR PDBsum; 4A1F; -. DR PDBsum; 4ZC0; -. DR AlphaFoldDB; O25916; -. DR SMR; O25916; -. DR DIP; DIP-3388N; -. DR IntAct; O25916; 4. DR MINT; O25916; -. DR STRING; 85962.HP_1362; -. DR PaxDb; 85962-C694_07030; -. DR EnsemblBacteria; AAD08402; AAD08402; HP_1362. DR KEGG; hpy:HP_1362; -. DR PATRIC; fig|85962.47.peg.1459; -. DR eggNOG; COG0305; Bacteria. DR InParanoid; O25916; -. DR OrthoDB; 9773982at2; -. DR PhylomeDB; O25916; -. DR EvolutionaryTrace; O25916; -. DR Proteomes; UP000000429; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1990077; C:primosome 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:0003678; F:DNA helicase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IBA:GO_Central. DR CDD; cd00984; DnaB_C; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR InterPro; IPR036185; DNA_heli_DnaB-like_N_sf. DR InterPro; IPR007692; DNA_helicase_DnaB. 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 NCBIfam; TIGR00665; DnaB; 1. DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1. DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1. DR Pfam; PF00772; DnaB; 1. DR Pfam; PF03796; DnaB_C; 1. DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS51199; SF4_HELICASE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; DNA replication; DNA-binding; Helicase; KW Hydrolase; Nucleotide-binding; Primosome; Reference proteome. FT CHAIN 1..488 FT /note="Replicative DNA helicase" FT /id="PRO_0000102023" FT DOMAIN 172..471 FT /note="SF4 helicase" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596" FT BINDING 203..210 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596" FT HELIX 3..23 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 25..27 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 28..32 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 37..39 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 43..57 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 64..69 FT /evidence="ECO:0007829|PDB:3GXV" FT STRAND 73..75 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 79..86 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 95..120 FT /evidence="ECO:0007829|PDB:3GXV" FT HELIX 154..171 FT /evidence="ECO:0007829|PDB:4A1F" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 184..190 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 198..203 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 209..222 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 226..234 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 236..248 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 252..257 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 262..277 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 280..283 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 290..303 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 307..316 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 321..326 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 331..345 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 349..354 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 357..361 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 362..364 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 369..371 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 372..374 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 383..389 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 391..407 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 408..410 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 412..431 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 434..445 FT /evidence="ECO:0007829|PDB:4A1F" FT STRAND 451..458 FT /evidence="ECO:0007829|PDB:4A1F" FT HELIX 459..461 FT /evidence="ECO:0007829|PDB:4A1F" FT TURN 469..471 FT /evidence="ECO:0007829|PDB:4A1F" SQ SEQUENCE 488 AA; 55726 MW; 6FF84C2DE4ED606F CRC64; MDHLKHLQQL QNIERIVLSG IVLANHKIEE VHSVLEPSDF YYPPNGLFFE IALKLHEEDC PIDENFIRQK MPKDKQIKEE DLVAIFAASP IDNIEAYVEE IKNASIKRKL FGLANTIREQ ALESAQKSSD ILGAVEREVY ALLNGSTIEG FRNIKEVLES AMDLITENQR KGSLEVTGIP TGFVQLDNYT SGFNKGSLVI IGARPSMGKT SLMMNMVLSA LNDDRGVAVF SLEMSAEQLA LRALSDLTSI NMHDLESGRL DDDQWENLAK CFDHLSQKKL FFYDKSYVRI EQIRLQLRKL KSQHKELGIA FIDYLQLMSG SKATKERHEQ IAEISRELKT LARELEIPII ALVQLNRSLE NRDDKRPILS DIKDSGGIEQ DADIVLFLYR GYIYQMRAED NKIDKLKKEG KIEEAQELYL KVNEERRIHK QNGSIEEAEI IVAKNRNGAT GTVYTRFNAP FTRYEDMPID SHLEEGQETK VDYDIVTT //