ID   A0A2C1AI71_BACCE        Unreviewed;       433 AA.
AC   A0A2C1AI71;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   07-OCT-2020, entry version 7.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=COC69_26165 {ECO:0000313|EMBL:PGS69054.1};
OS   Bacillus cereus.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=1396 {ECO:0000313|EMBL:PGS69054.1, ECO:0000313|Proteomes:UP000224203};
RN   [1] {ECO:0000313|EMBL:PGS69054.1, ECO:0000313|Proteomes:UP000224203}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS041711 {ECO:0000313|EMBL:PGS69054.1,
RC   ECO:0000313|Proteomes:UP000224203};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC       {ECO:0000256|ARBA:ARBA00008428}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PGS69054.1}.
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DR   EMBL; NULI01000168; PGS69054.1; -; Genomic_DNA.
DR   Proteomes; UP000224203; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.860.10; -; 1.
DR   InterPro; IPR036185; DNA_heli_DnaB-like_N_sf.
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   PROSITE; PS51199; SF4_HELICASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000313|EMBL:PGS69054.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          164..433
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   433 AA;  50177 MW;  12DBC51EB3CD954C CRC64;
     MEKYQRYAEN ELYMLGCLMK DNTLFEELRL TGEHFIHVQH KQLFQAMMEL WQEEKPINDV
     SLSQVSGKQI KSFGGVSKIY ECHRQALTLH NFQFIQQKMM EFIAVDDILV DIKEFERKTE
     DRHSLKDLNE LVTKVNKIQI ATVKPQLSFQ AKLQMRVEEH IQMQASGLSG TNTGFANINH
     FMDGWQPTDL IVVAARPSVG KTAITLDTMR KGAKADPKRY MGTFFSCEMI ESKVIDRWIA
     AEGRLPVNEL SNPNKFFGQD EKKWKKYQMA TADLSTLPIN IRSEKHMNEI KAVIWKIVKD
     YPDKKHLFVI DHLGHIKTDE SFVSNHLKFT YIINELKDIQ KAVEQPIILI AQLNRAVEGK
     QDKRPSMSDI RESGSIEEVA DVIIFPHRDA YFDKDRRESE EIHETELIVA KNRNGAVGTL
     TLNFVKRTNE FVE
//