ID A0A1W7QSI8_9BACT Unreviewed; 449 AA. AC A0A1W7QSI8; DT 05-JUL-2017, integrated into UniProtKB/TrEMBL. DT 05-JUL-2017, sequence version 1. DT 02-OCT-2024, entry version 22. DE RecName: Full=Replicative DNA helicase {ECO:0000256|NCBIfam:TIGR00665, ECO:0000256|RuleBase:RU362085}; DE EC=5.6.2.3 {ECO:0000256|NCBIfam:TIGR00665, ECO:0000256|RuleBase:RU362085}; GN ORFNames=GPEL0_01f2444 {ECO:0000313|EMBL:GAW66891.1}; OS Geoanaerobacter pelophilus. OC Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales; OC Geobacteraceae; Geoanaerobacter. OX NCBI_TaxID=60036 {ECO:0000313|EMBL:GAW66891.1, ECO:0000313|Proteomes:UP000194153}; RN [1] {ECO:0000313|EMBL:GAW66891.1, ECO:0000313|Proteomes:UP000194153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Drf2 {ECO:0000313|EMBL:GAW66891.1, RC ECO:0000313|Proteomes:UP000194153}; RG Geobacter pelophilus Genome Sequencing; RA Aoyagi T., Koike H., Hori T.; RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:GAW66891.1, ECO:0000313|Proteomes:UP000194153} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Drf2 {ECO:0000313|EMBL:GAW66891.1, RC ECO:0000313|Proteomes:UP000194153}; RA Aoyagi T., Koike H., Morita T., Sato Y., Habe H., Hori T.; RT "Draft genome sequence of Geobacter pelophilus, a iron(III)-reducing RT bacteria."; RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: The main replicative DNA helicase, it participates in CC initiation and elongation during chromosome replication. Travels ahead CC of the DNA replisome, separating dsDNA into templates for DNA CC synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA- CC dependent ATPase activity. {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=5.6.2.3; CC Evidence={ECO:0000256|ARBA:ARBA00044904, CC ECO:0000256|RuleBase:RU362085}; CC -!- CATALYTIC ACTIVITY: CC Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA at the CC replication fork by translocating in the 5'-3' direction. This CC creates two antiparallel DNA single strands (ssDNA). The leading CC ssDNA polymer is the template for DNA polymerase III holoenzyme which CC synthesizes a continuous strand.; EC=5.6.2.3; CC Evidence={ECO:0000256|ARBA:ARBA00044875, 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:GAW66891.1}. 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; BDQG01000001; GAW66891.1; -; Genomic_DNA. DR AlphaFoldDB; A0A1W7QSI8; -. DR OrthoDB; 9773982at2; -. DR Proteomes; UP000194153; 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 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:GAW66891.1}; 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:UP000194153}. FT DOMAIN 179..447 FT /note="SF4 helicase" FT /evidence="ECO:0000259|PROSITE:PS51199" SQ SEQUENCE 449 AA; 50356 MW; 5A246901041706C9 CRC64; MNATDMRKLP PQSIEAEMSI LGGILVDNEA INRVLEILVP DDLYRESHRK ILRAMIELNE RGEPCDLITM TTILRKKGEL EEVGGGAYLA TLVDFVPMAA NISYYCKIVK EKWLTRKLIS AATDIVSKGF EDKVDTEELL DAAQKVIFEI SENKIRPAYY QVSDILKDTI KNIELLYEKK ELVTGVPTGY TDLDKLTAGF HAGDLVIIAG RPAMGKTTFA LNVAQYAAID ADQAYPAAVF SLEMPKEQLV ERLLCSVAKV DLSRLRSGHL VENDWPKLIK AGGKLHDAKI FIDDTPSITI MELRSKARRL KAEHNIGLIV IDYLQLMRGG ANPESRQQEI SEISRSLKGL AKELSIPVIA LSQLNRGLEQ RSDKRPMMSD LRESGAIEQD ADIIMFVYRE EVYEKDKEDL KGKAEVIIGK HRSGPTGTVH LAFRGEFTRF ENLSSRDDY //