ID A0A437PWE0_9BACT Unreviewed; 530 AA.
AC A0A437PWE0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=dnaB {ECO:0000313|EMBL:RVU26585.1};
GN ORFNames=EOJ36_00910 {ECO:0000313|EMBL:RVU26585.1};
OS Sandaracinomonas limnophila.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Sandaracinomonas.
OX NCBI_TaxID=1862386 {ECO:0000313|EMBL:RVU26585.1, ECO:0000313|Proteomes:UP000282832};
RN [1] {ECO:0000313|EMBL:RVU26585.1, ECO:0000313|Proteomes:UP000282832}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSY-15 {ECO:0000313|EMBL:RVU26585.1,
RC ECO:0000313|Proteomes:UP000282832};
RA Chen W.-M.;
RL Submitted (JAN-2019) 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:RVU26585.1}.
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DR EMBL; SACY01000001; RVU26585.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A437PWE0; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000282832; 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:RVU26585.1};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000282832}.
FT DOMAIN 205..480
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 509..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 530 AA; 58745 MW; 12756DE3018E143B CRC64;
MEINSSSNQV RRGNSSGISR SNGPVRLGDL GLGKLPPQAV DLEEALLGAL MLEKEPLTNV
IELLKPDSFY KEAHQKIFQA IQGLFQASQP VDLLTVHNYL KTNGNLEATG GASYLAQLTS
RVSSSSNVEF HARIIIEQYL KRQLISISSE IQKLSYEDTS DVFQILDKME QELFTIAESN
IRKNYESMSD ILKKAVDELE KKQLQKSGLT GIPSGFTALD RLTSGFQRQE LIIIAARPGM
GKTAFVVSAC RNAAVEFDKP VALFSLEMSG VQLVNRIISA EAEIESEKIR KGKLEPHEWQ
QLHTKIKKLY DAPIYIDDTP ALSILELRAK CRRLKAQKNI ELVVIDYLQL MTGDSSGKGP
SGNREQEISQ ISRALKQLAK ELDIPVIALS QLNRSTETRG GNKKPQLSDL RESGAIEQDA
DQVMFIYRPD YYGITQDDSG NSVMGMGEII MAKNRSGSLE NVWLKFIGKY TKYCDLDADQ
FEGNLGNLGN LGDTSGDFDN AKEESIFKGS KLNNSNAAPS ADFDPFEEPM
//
