ID   DNAB_ECO57              Reviewed;         471 AA.
AC   Q8X5V3; Q7A929;
DT   08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=Replicative DNA helicase;
DE            EC=3.6.4.12;
GN   Name=dnaB; OrderedLocusNames=Z5650, ECs5034;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SUBUNIT: Homohexamer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AE005174; AAG59250.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB38457.1; -; Genomic_DNA.
DR   PIR; B91258; B91258.
DR   PIR; F86098; F86098.
DR   RefSeq; NP_313061.1; NC_002695.1.
DR   RefSeq; WP_000918366.1; NZ_SWKA01000005.1.
DR   AlphaFoldDB; Q8X5V3; -.
DR   BMRB; Q8X5V3; -.
DR   SMR; Q8X5V3; -.
DR   STRING; 155864.EDL933_5388; -.
DR   EnsemblBacteria; AAG59250; AAG59250; Z5650.
DR   EnsemblBacteria; BAB38457; BAB38457; ECs_5034.
DR   GeneID; 914301; -.
DR   KEGG; ece:Z5650; -.
DR   KEGG; ecs:ECs_5034; -.
DR   PATRIC; fig|386585.9.peg.5257; -.
DR   eggNOG; COG0305; Bacteria.
DR   HOGENOM; CLU_005373_0_0_6; -.
DR   OMA; IEFHARI; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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; IPR003593; AAA+_ATPase.
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   SMART; SM00382; AAA; 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; Reference proteome.
FT   CHAIN           1..471
FT                   /note="Replicative DNA helicase"
FT                   /id="PRO_0000102020"
FT   DOMAIN          200..467
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         231..238
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ   SEQUENCE   471 AA;  52406 MW;  6C3CA344AFB1DC62 CRC64;
     MAGNKPFNKQ QAEPRERDPQ VAGLKVPPHS IEAEQSVLGG LMLDNERWDD VAERVVADDF
     YTRPHRHIFT EMARLQESGS PIDLITLAES LERQGQLDSV GGFAYLAELS KNTPSAANIS
     SYADIVRERA VVREMISVAN EIAEAGFDPQ GRTSEDLLDL AESRVFKIAE SRANKDEGPK
     NIADVLDATV ARIEQLFQQP HDGVTGVNTG YDDLNKKTAG LQPSDLIIVA ARPSMGKTTF
     AMNLVENAAM LQDKPVLIFS LEMPSEQIMM RSLASLSRVD QTKIRTGQLD DEDWARISGT
     MGILLEKRNI YIDDSSGLTP TEVRSRARRI AREHGGIGLI MIDYLQLMRV PALSDNRTLE
     IAEISRSLKA LAKELNVPVV ALSQLNRSLE QRADKRPVNS DLRESGSIEQ DADLIMFIYR
     DEVYHENSDL KGIAEIIIGK QRNGPIGTVR LTFNGQWSRF DNYAGPQYDD E