ID   DNAB_SHIFL              Reviewed;         471 AA.
AC   P0ACB1; P03005;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Replicative DNA helicase;
DE            EC=3.6.4.12;
GN   Name=dnaB; OrderedLocusNames=SF4154, S3577;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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}.
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; AE005674; AAN45575.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18623.1; -; Genomic_DNA.
DR   RefSeq; NP_709868.1; NC_004337.2.
DR   RefSeq; WP_000918363.1; NZ_WPGW01000163.1.
DR   AlphaFoldDB; P0ACB1; -.
DR   BMRB; P0ACB1; -.
DR   SMR; P0ACB1; -.
DR   STRING; 198214.SF4154; -.
DR   EnsemblBacteria; AAN45575; AAN45575; SF4154.
DR   EnsemblBacteria; AAP18623; AAP18623; S3577.
DR   GeneID; 1025050; -.
DR   GeneID; 66672034; -.
DR   KEGG; sfl:SF4154; -.
DR   KEGG; sfx:S3577; -.
DR   PATRIC; fig|198214.7.peg.4900; -.
DR   HOGENOM; CLU_005373_0_0_6; -.
DR   OMA; IEFHARI; -.
DR   OrthoDB; 1709134at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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_0000102032"
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;  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