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Database: UniProt
Entry: A0A1G8CKS4_9BURK
LinkDB: A0A1G8CKS4_9BURK
Original site: A0A1G8CKS4_9BURK 
ID   A0A1G8CKS4_9BURK        Unreviewed;       469 AA.
AC   A0A1G8CKS4;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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=SAMN05444748_101419 {ECO:0000313|EMBL:SDH46137.1};
OS   Variovorax sp. OV700.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1882826 {ECO:0000313|EMBL:SDH46137.1, ECO:0000313|Proteomes:UP000199505};
RN   [1] {ECO:0000313|Proteomes:UP000199505}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV700 {ECO:0000313|Proteomes:UP000199505};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00003574, 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}.
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DR   EMBL; FNDR01000001; SDH46137.1; -; Genomic_DNA.
DR   RefSeq; WP_055804819.1; NZ_FNDR01000001.1.
DR   AlphaFoldDB; A0A1G8CKS4; -.
DR   STRING; 1882826.SAMN05444748_101419; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000199505; 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|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
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}.
FT   DOMAIN          196..464
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   469 AA;  51697 MW;  407FE7ADEA342E26 CRC64;
     MSAVFSYADN DPSADRQVAK LRIPPHSIEA ESSVLGGLLL DNGAWDRMGD LLVDGDFYRH
     EHKLIYAAIG GLINASKPAD VITVYEQLQG LGKAEEIGGL VYLNSLAQYV PSASNIRRYA
     EIVRERSILR KLVSASDEIA TNAFNTQGKS VDKILDEAEQ KIFNIGEEGT RMKQGFQSMD
     ALVVELLDRV TEMAENPNDI TGVRTGFYEF DKMTSGLQPG DMIVLAARPS MGKTSLAINI
     AEHVALNEGL PVAVFSMEMG ASQLAVRIVG SIGRIDQGHL RTGKLSDEEW PRLTEAIEKL
     RNVSLHIDET PGLTTSELRA NARRLARQYG RLGLIVVDYL QLMSVSTSMN DENRATAVGE
     ISRGLKMLAK ELKCPVIALS QLSRGVESRT DKRPMMSDLR ESGAIEQDAD IIMFIYRDDY
     YDKNSKEPGV AEVIISKHRN GPTGTVKLTF LKPLTKFENM ASYGSNDDY
//
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