DNAB_ECOLI
ID DNAB_ECOLI Reviewed; 471 AA.
AC P0ACB0; P03005; Q2M6Q2;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; Synonyms=groP, grpA; OrderedLocusNames=b4052, JW4012;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6323420; DOI=10.1016/s0021-9258(17)43626-x;
RA Nakayama N., Arai N., Bond M.W., Kaziro Y., Arai K.;
RT "Nucleotide sequence of dnaB and the primary structure of the dnaB protein
RT from Escherichia coli.";
RL J. Biol. Chem. 259:97-101(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=8265357; DOI=10.1093/nar/21.23.5408;
RA Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.;
RT "Analysis of the Escherichia coli genome. IV. DNA sequence of the region
RT from 89.2 to 92.8 minutes.";
RL Nucleic Acids Res. 21:5408-5417(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RC STRAIN=K12;
RA Dixon N.E., Lilley P.E.;
RT "E. coli homolog of zeta crystallin.";
RL Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [8]
RP STRUCTURE BY NMR OF 24-137.
RX PubMed=10404597; DOI=10.1016/s0969-2126(99)80089-6;
RA Weigelt J., Brown S.E., Miles C.S., Dixon N.E., Otting G.;
RT "NMR structure of the N-terminal domain of E. coli DnaB helicase:
RT implications for structure rearrangements in the helicase hexamer.";
RL Structure 7:681-690(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 -!- 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.
CC -!- INTERACTION:
CC P0ACB0; P03004: dnaA; NbExp=4; IntAct=EBI-548978, EBI-548951;
CC P0ACB0; P0ACB0: dnaB; NbExp=6; IntAct=EBI-548978, EBI-548978;
CC P0ACB0; P0AEF0: dnaC; NbExp=12; IntAct=EBI-548978, EBI-549012;
CC P0ACB0; P0ABS5: dnaG; NbExp=3; IntAct=EBI-548978, EBI-549259;
CC P0ACB0; P06710: dnaX; NbExp=2; IntAct=EBI-548978, EBI-549140;
CC P0ACB0; P23862: priC; NbExp=5; IntAct=EBI-548978, EBI-1117383;
CC P0ACB0; P09980: rep; NbExp=3; IntAct=EBI-548978, EBI-6558011;
CC -!- INDUCTION: Slightly induced by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; K01174; AAA23689.1; -; Genomic_DNA.
DR EMBL; L02312; AAA23690.1; -; Genomic_DNA.
DR EMBL; U00006; AAC43146.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77022.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78054.1; -; Genomic_DNA.
DR PIR; C65213; IQECDB.
DR RefSeq; NP_418476.1; NC_000913.3.
DR RefSeq; WP_000918363.1; NZ_STEB01000022.1.
DR PDB; 1B79; X-ray; 2.30 A; A/B/C/D=16-129.
DR PDB; 1JWE; NMR; -; A=24-137.
DR PDB; 6BBM; EM; 4.10 A; A/B/C/D/E/F=1-471.
DR PDB; 6KZA; X-ray; 3.10 A; A/B=180-471.
DR PDB; 6QEL; EM; 3.90 A; A/B/C/D/E/F=1-471.
DR PDB; 6QEM; EM; 3.40 A; A/B/C/D/E/F=1-471.
DR PDBsum; 1B79; -.
DR PDBsum; 1JWE; -.
DR PDBsum; 6BBM; -.
DR PDBsum; 6KZA; -.
DR PDBsum; 6QEL; -.
DR PDBsum; 6QEM; -.
DR AlphaFoldDB; P0ACB0; -.
DR BMRB; P0ACB0; -.
DR SMR; P0ACB0; -.
DR BioGRID; 4261652; 171.
DR BioGRID; 852849; 4.
DR ComplexPortal; CPX-1933; DnaB-DnaG primase-helicase complex.
DR ComplexPortal; CPX-1934; dnaB-dnaC complex.
DR ComplexPortal; CPX-1946; dnaB helicase complex.
DR ComplexPortal; CPX-1950; dnaA-dnaB-dnaC loader complex.
DR ComplexPortal; CPX-1951; Replication restart pre-primosome complex, priAB variant.
DR ComplexPortal; CPX-1952; Replication restart pre-primosome complex, priAC variant.
DR ComplexPortal; CPX-1953; Replication restart pre-primosome complex priC-rep variant.
DR ComplexPortal; CPX-5909; Replication restart primosome complex, priAC variant.
DR ComplexPortal; CPX-5910; Replication restart primosome complex, priAB variant.
DR ComplexPortal; CPX-5911; Replication restart primosome complex, priC-rep variant.
DR DIP; DIP-9456N; -.
DR IntAct; P0ACB0; 39.
DR MINT; P0ACB0; -.
DR STRING; 511145.b4052; -.
DR SWISS-2DPAGE; P0ACB0; -.
DR jPOST; P0ACB0; -.
DR PaxDb; P0ACB0; -.
DR PRIDE; P0ACB0; -.
DR EnsemblBacteria; AAC77022; AAC77022; b4052.
DR EnsemblBacteria; BAE78054; BAE78054; BAE78054.
DR GeneID; 66672034; -.
DR GeneID; 948555; -.
DR KEGG; ecj:JW4012; -.
DR KEGG; eco:b4052; -.
DR PATRIC; fig|1411691.4.peg.2655; -.
DR EchoBASE; EB0232; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_0_0_6; -.
DR InParanoid; P0ACB0; -.
DR OMA; IEFHARI; -.
DR PhylomeDB; P0ACB0; -.
DR BioCyc; EcoCyc:EG10236-MON; -.
DR BioCyc; MetaCyc:EG10236-MON; -.
DR EvolutionaryTrace; P0ACB0; -.
DR PRO; PR:P0ACB0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0033202; C:DNA helicase complex; IDA:ComplexPortal.
DR GO; GO:1990100; C:DnaB-DnaC complex; IPI:ComplexPortal.
DR GO; GO:1990158; C:DnaB-DnaC-DnaT-PriA-PriB complex; IC:ComplexPortal.
DR GO; GO:1990159; C:DnaB-DnaC-DnaT-PriA-PriC complex; IC:ComplexPortal.
DR GO; GO:1990160; C:DnaB-DnaC-Rep-PriC complex; IC:ComplexPortal.
DR GO; GO:1990156; C:DnaB-DnaG complex; IPI:ComplexPortal.
DR GO; GO:1990077; C:primosome complex; IC:ComplexPortal.
DR GO; GO:0030894; C:replisome; IC:ComplexPortal.
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; IDA:EcoCyc.
DR GO; GO:0004386; F:helicase activity; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0032508; P:DNA duplex unwinding; IDA:ComplexPortal.
DR GO; GO:0006260; P:DNA replication; IMP:EcoCyc.
DR GO; GO:0006270; P:DNA replication initiation; IDA:ComplexPortal.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IDA:ComplexPortal.
DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IDA:EcoCyc.
DR GO; GO:0031297; P:replication fork processing; IC:ComplexPortal.
DR GO; GO:0010212; P:response to ionizing radiation; IMP:EcoCyc.
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 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..471
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102019"
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:0000305"
FT HELIX 30..43
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 45..47
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 48..52
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:1B79"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 63..77
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 84..92
FT /evidence="ECO:0007829|PDB:1B79"
FT TURN 93..96
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 102..112
FT /evidence="ECO:0007829|PDB:1B79"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 119..127
FT /evidence="ECO:0007829|PDB:1B79"
FT HELIX 155..170
FT /evidence="ECO:0007829|PDB:6QEM"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:6QEM"
FT HELIX 182..197
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 205..207
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 226..230
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 233..235
FT /evidence="ECO:0007829|PDB:6QEM"
FT HELIX 237..250
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 261..263
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 281..285
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 291..307
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 320..333
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 338..343
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 345..347
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 379..383
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 387..391
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:6KZA"
FT TURN 403..405
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 408..411
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 413..419
FT /evidence="ECO:0007829|PDB:6KZA"
FT HELIX 421..424
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 431..444
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 447..454
FT /evidence="ECO:0007829|PDB:6KZA"
FT TURN 455..458
FT /evidence="ECO:0007829|PDB:6KZA"
FT STRAND 459..462
FT /evidence="ECO:0007829|PDB:6KZA"
SQ SEQUENCE 471 AA; 52390 MW; 5B5ED3625A7F7DE5 CRC64;
MAGNKPFNKQ QAEPRERDPQ VAGLKVPPHS IEAEQSVLGG LMLDNERWDD VAERVVADDF
YTRPHRHIFT EMARLQESGS PIDLITLAES LERQGQLDSV GGFAYLAELS KNTPSAANIS
AYADIVRERA 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
