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Database: UniProt
Entry: A0A2U3AAM6_9BACL
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ID   A0A2U3AAM6_9BACL        Unreviewed;       448 AA.
AC   A0A2U3AAM6;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   27-MAR-2024, entry version 25.
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   Name=dnaC {ECO:0000313|EMBL:STX11244.1};
GN   ORFNames=NCTC10597_03054 {ECO:0000313|EMBL:STX11244.1};
OS   Kurthia zopfii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Kurthia.
OX   NCBI_TaxID=1650 {ECO:0000313|EMBL:STX11244.1, ECO:0000313|Proteomes:UP000254330};
RN   [1] {ECO:0000313|EMBL:STX11244.1, ECO:0000313|Proteomes:UP000254330}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10597 {ECO:0000313|EMBL:STX11244.1,
RC   ECO:0000313|Proteomes:UP000254330};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) 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|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:STX11244.1}.
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DR   EMBL; UGNP01000001; STX11244.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U3AAM6; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000254330; 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:InterPro.
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; 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   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   SMART; SM00382; AAA; 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:STX11244.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362085};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|RuleBase:RU362085};
KW   Primosome {ECO:0000256|ARBA:ARBA00022515, ECO:0000256|RuleBase:RU362085}.
SQ   SEQUENCE   448 AA;  49678 MW;  702A220BC56BB6F9 CRC64;
     MNDPTTDRIP PHNQEAEQSV LGAVFLEPQA LITASETLLS EDFYQAAHRM IFDSMLRLSD
     MGKAVDVVTV INELDSRNEL DDVGGVSYMT ELANAVPTAA NVAYYSEIVA QKALLRRLIH
     TATKIVEDTF AREDEVEALL AEAEKKIMEV ASRSNSSDFK HVKDVLVQTY ENVEKLQNRK
     GDITGIPTGF RDLDRLTAGF QRGDLIIVAA RPSVGKTAFA LNVAQAVGTQ TTENVAIFSL
     EMGAEQLVMR MLCAEGNIDA QVLRTGALTT EDWRKLTMAM GSLSRAGIYI DDAAGVRVNE
     IRAKCRRLKQ ESGLGMILID YLQLIQGSGS SGQNRQQEVS EISRSLKALA RELEVPVIAL
     SQLSRGVEQR QDKRPMMSDL RESGSIEQDA DIVAFLYRED YYDKETEDAN TIEIIVAKQR
     NGPTDTVKLA FKKEFNKFVS VDWSQESP
//
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