DNAB_HELPJ
ID DNAB_HELPJ Reviewed; 486 AA.
AC Q9ZJM5;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=jhp_1280;
OS Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J99 / ATCC 700824;
RX PubMed=9923682; DOI=10.1038/16495;
RA Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT "Genomic sequence comparison of two unrelated isolates of the human gastric
RT pathogen Helicobacter pylori.";
RL Nature 397:176-180(1999).
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 -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001439; AAD06865.1; -; Genomic_DNA.
DR PIR; F71825; F71825.
DR RefSeq; WP_000349702.1; NZ_CP011330.1.
DR AlphaFoldDB; Q9ZJM5; -.
DR SMR; Q9ZJM5; -.
DR STRING; 85963.jhp_1280; -.
DR EnsemblBacteria; AAD06865; AAD06865; jhp_1280.
DR KEGG; hpj:jhp_1280; -.
DR PATRIC; fig|85963.30.peg.1288; -.
DR eggNOG; COG0305; Bacteria.
DR OMA; WENLAKC; -.
DR Proteomes; UP000000804; Chromosome.
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; IEA:UniProtKB-EC.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; 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; 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 Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome.
FT CHAIN 1..486
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102024"
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"
SQ SEQUENCE 486 AA; 55540 MW; 79FBC5779A83624B CRC64;
MDHLKHLQQL QNIERIVLSG IVLANHKIEE IHSVLEPSDF YYPPHGLFFE IALKLHEVNC
PIDENFIRQK MPKDKQISED DLVAIFAASP IDNIEAYVEE IKNASIKRKL FTLANTIREQ
ALESAQKSSD ILNAVEREVY ALLNGSTIEG FRGIKEVLES TMNLITENQR KGSLKVTGIP
TGFVQLDNYT SGFNQGSLVI LGARPSMGKT SLMMNMVLSA LNDDRGVAVF SLEMSAEQLA
LRALSDLTSI NMHDLESARL DDDQWENLAK CFDHLSQKKL FFYDKSYVRM DQIRLQLRKL
KSQHKELGIA FIDYLQLMSG NKATKERHEQ IAEISRELKT LARELEIPII ALVQLNRSLE
NRDDKRPILS DIKDSGGIEQ DADIVLFLYR GYIYQMRAED NKIDKLKKEG KVEEAQELHL
KVNEERRIHK QNGSIEEAEI IVAKNRNGAT GTVYTRFNAP FTRYEDMPVD SHLEEGQETK
FEMPTT