ID A0A087B2N9_9BIFI Unreviewed; 454 AA.
AC A0A087B2N9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Replicative DNA helicase {ECO:0000256|ARBA:ARBA00021957, ECO:0000256|RuleBase:RU362085};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|RuleBase:RU362085};
GN ORFNames=BCUN_1055 {ECO:0000313|EMBL:KFI65289.1};
OS Bifidobacterium cuniculi.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1688 {ECO:0000313|EMBL:KFI65289.1, ECO:0000313|Proteomes:UP000029067};
RN [1] {ECO:0000313|EMBL:KFI65289.1, ECO:0000313|Proteomes:UP000029067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 10738 {ECO:0000313|EMBL:KFI65289.1,
RC ECO:0000313|Proteomes:UP000029067};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Participates in initiation and elongation during chromosome
CC replication; it exhibits DNA-dependent ATPase activity.
CC {ECO:0000256|ARBA:ARBA00002835, ECO:0000256|RuleBase:RU362085}.
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 ECO:0000256|RuleBase:RU362085};
CC -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000256|ARBA:ARBA00008428, ECO:0000256|RuleBase:RU362085}.
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:KFI65289.1}.
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DR EMBL; JGYV01000002; KFI65289.1; -; Genomic_DNA.
DR RefSeq; WP_033517209.1; NZ_JGYV01000002.1.
DR AlphaFoldDB; A0A087B2N9; -.
DR STRING; 1688.BCUN_1055; -.
DR eggNOG; COG0305; Bacteria.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000029067; Unassembled WGS sequence.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-UniRule.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
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 NCBIfam; TIGR00665; DnaB; 1.
DR PANTHER; PTHR30153:SF2; REPLICATIVE DNA HELICASE; 1.
DR PANTHER; PTHR30153; REPLICATIVE DNA HELICASE DNAB; 1.
DR Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; N-terminal domain of DnaB helicase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU362085};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW ECO:0000256|RuleBase:RU362085};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU362085};
KW Helicase {ECO:0000256|RuleBase:RU362085, ECO:0000313|EMBL:KFI65289.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU362085}; Primosome {ECO:0000256|RuleBase:RU362085};
KW Reference proteome {ECO:0000313|Proteomes:UP000029067}.
FT DOMAIN 185..450
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
SQ SEQUENCE 454 AA; 50195 MW; E1646810B2DC4CF3 CRC64;
MSDEFPTNSS LFDRVPPHDD DAEMATLGGM LLSKDAIGEV SQTIEVADFY QPKHQTIYEA
IIDLFAASLP VDAVTVANKL NDEGNLEKVG GPDYLHSLIA SVPTAANAIY YAEIVHQRAL
LRQVIVAGTK ITQLGYSAEG SQAQDVINLA QAEVYEMSMG RVRQDYTPIK AAVEAALDQL
DRIQKGEIET GIMTGFRDID AVTKGLQPGQ MVVVAGRPAM GKSTLGVDFA RAAALHQGLT
SVIFSLEMSK MELAQRIISA ETNIPLAAMR NPEDIDPGRW NTLNNFFGKL ENAPLFIDDS
PNMSLMEIRA KCRRLKQTND LKLVVIDYLQ LMSSGKQVES RQQEVSEFSR ALKLLAKELE
VPVVALSQLN RSSEMRNDKK PQLSDLRESG SIEQDADVVF LVHRPDAYDK EDRPGEADII
MAKHRNGPTD TFNLAFRGQY SKFQDMPQDY QQGV
//
