ID   DNAB_SALTY              Reviewed;         471 AA.
AC   P0A1Q4; P10338;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Replicative DNA helicase;
DE            EC=3.6.4.12;
GN   Name=dnaB; OrderedLocusNames=STM4246;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2836367; DOI=10.1128/jb.170.6.2668-2675.1988;
RA   Wong A., Kean L., Maurer R.;
RT   "Sequence of the dnaB gene of Salmonella typhimurium.";
RL   J. Bacteriol. 170:2668-2675(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(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   -!- 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   -!- 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; J03390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AE006468; AAL23070.1; -; Genomic_DNA.
DR   PIR; A32011; A32011.
DR   RefSeq; NP_463111.1; NC_003197.2.
DR   RefSeq; WP_000918353.1; NC_003197.2.
DR   AlphaFoldDB; P0A1Q4; -.
DR   SMR; P0A1Q4; -.
DR   STRING; 99287.STM4246; -.
DR   PaxDb; P0A1Q4; -.
DR   EnsemblBacteria; AAL23070; AAL23070; STM4246.
DR   GeneID; 1255772; -.
DR   KEGG; stm:STM4246; -.
DR   PATRIC; fig|99287.12.peg.4466; -.
DR   HOGENOM; CLU_005373_0_0_6; -.
DR   OMA; IEFHARI; -.
DR   PhylomeDB; P0A1Q4; -.
DR   BioCyc; SENT99287:STM4246-MON; -.
DR   Proteomes; UP000001014; 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: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; 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_0000102031"
FT   DOMAIN          200..467
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT   REGION          1..22
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"
SQ   SEQUENCE   471 AA;  52687 MW;  46C3C5ECD937A573 CRC64;
     MAGNKPFNKP QTDARDRDPQ VAGIKVPPHS IEAEQSVLGG LMLDNERWDD VAERVVAEDF
     YTRPHRHIFT EMGRLQESGS PIDLITLAES LERQGQLDSV GGFAYLAELS KNTPSAANIS
     AYADIVRERA VVRDMIAVAH EIADAGYDPQ GRNSDELLDL AESRVFQIAE NRANKDEGPK
     SIDQILDATV ARIEQLFQQP HDGVTGVDTG YQDLNKKTAG LQRSDLIIVA ARPSMGKTTF
     AMNLCENAAM LQDKPVLIFS LEMPGEQIMM RMLASLSRVD QTRIRTGQLD DEDWARISGT
     MGILLEKRNM YIDDSSGLTP TEVRSRARRI FREHGGLSLI MIDYLQLMRV PSLSDNRTLE
     IAEISRSLKA LAKELQVPVV ALSQLNRSLE QRADKRPVNS DLRESGSIEQ DADLIMFIYR
     DEVYHENSDL KGIAEIIIGK QRNGPIGTVR LTFNGQWSRF DNYAGPQYDD E