ID S7WRK6_9BACT Unreviewed; 526 AA.
AC S7WRK6;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=ADICYQ_1619 {ECO:0000313|EMBL:EPR69374.1};
OS Cyclobacterium qasimii M12-11B.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC Cyclobacterium.
OX NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR69374.1, ECO:0000313|Proteomes:UP000014974};
RN [1] {ECO:0000313|EMBL:EPR69374.1, ECO:0000313|Proteomes:UP000014974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M12-11B {ECO:0000313|EMBL:EPR69374.1,
RC ECO:0000313|Proteomes:UP000014974};
RX PubMed=23950138;
RA Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT from Arctic Marine Sediment.";
RL Genome Announc. 1:e00642-13(2013).
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:EPR69374.1}.
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DR EMBL; ATNM01000066; EPR69374.1; -; Genomic_DNA.
DR RefSeq; WP_020893417.1; NZ_ATNM01000066.1.
DR AlphaFoldDB; S7WRK6; -.
DR STRING; 641524.ADICYQ_1619; -.
DR PATRIC; fig|641524.5.peg.1607; -.
DR eggNOG; COG0305; Bacteria.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000014974; 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:EPR69374.1};
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}.
FT DOMAIN 199..472
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 483..526
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 526 AA; 58097 MW; AA6DFA94907A0EF1 CRC64;
MSDNNSNRSE RKTSNRRRPN ESFSALGKLP PQAIDMEEAV LGALMLEKDA LTTVVDILSP
GSFYRDSHSL IFEAILDLFN AGEPVDLLTV VNQLRKNGSL ELAGGVIYIT ELTSKVSSAS
NIEYHARVIT EQAMKRDMIK ISSEIQKEAF EDTTDVFELL DKMEQSLFEI SENNIKKNYV
DMRSIMREAI VELEGKKGQK DGLTGVPSGF TALDRVTSGW QKSDLVIIAA RPAMGKTAFV
LSVLRNAAVD HDRPVAIFSL EMSAIQLVNR LISSEAELDS EKIKKGNLAD YEWQQLIHKT
GKLTSAPFFV DDTPALSILE LRAKCRRLKA QNDIQMIVID YLQLMSGDSK GGGGNREQEI
SSISRALKQI AKELSVPVIA LSQLSRAVET RGGDKRPQLS DLRESGAIEQ DADIVMFLYR
PEYYGITEDE DGNNTAGVGE VIIAKHRNGS LENVKLRFIG KYTKFTDLEI NVPYQQPQEA
LYGSRFPSNA TGKGFDEEGM VRMGSKANGD QGGENPFPGG NEPAPF
//
