ID A0A2T7BN01_9BACT Unreviewed; 527 AA.
AC A0A2T7BN01;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-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 Name=dnaB {ECO:0000313|EMBL:PUZ29058.1};
GN ORFNames=DCC81_06200 {ECO:0000313|EMBL:PUZ29058.1};
OS Chitinophaga parva.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2169414 {ECO:0000313|EMBL:PUZ29058.1, ECO:0000313|Proteomes:UP000244450};
RN [1] {ECO:0000313|EMBL:PUZ29058.1, ECO:0000313|Proteomes:UP000244450}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY-1 {ECO:0000313|EMBL:PUZ29058.1,
RC ECO:0000313|Proteomes:UP000244450};
RA Chen K.;
RT "Chitinophaga fuyangensis sp. nov., isolated from soil in a chemical
RT factory.";
RL Submitted (APR-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:PUZ29058.1}.
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DR EMBL; QCYK01000001; PUZ29058.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T7BN01; -.
DR OrthoDB; 9773982at2; -.
DR Proteomes; UP000244450; 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:PUZ29058.1};
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:UP000244450}.
FT DOMAIN 197..474
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT REGION 469..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 527 AA; 58769 MW; CCAFA7FA8CEABACE CRC64;
MDLNLKKDRN VRRKPAVDVS TQIYGKVPPQ SKELEEAVLG AIMLEKGAFD TVVEILKSDC
FYVEAHKKIF LAMIRLAGKS MPVDILTVVE ELRFMGELDL VGGPFYVSQL TNSVVSSANV
EAHARIILQK FIQRELIRIS GEILSESYED TADVFDLLDS AESKLFEITN NHLRKNYDSI
DRVLVNTMKR IEDLRNKGDD ITGVPSGFPS LDKVTYGWQP TDLIILAARP AVGKTAFALN
LVRNAALHPR FPKGAAIFSL EMSSGQLVAR ILAAEAEIKL EKITRGKLEE YEMKKLMTHG
VERLAKAPIF VDDTPALNIF ELRAKCRRLV HNNGVGIIII DYLQLMSGSA DGKNTNREQE
ISKISRELKG LAKELQVPVI ALSQLSRDVE KRKDGNKMPQ LSDLRESGAI EQDADMVLFL
YRPEYYDINQ NEMGESNKGE THVRIAKHRN GQLDTIKLRA VLEYQRFEDD GSLENPGGPS
FPGGGGNSFA GMRPGSGDND EAKLYIQKGS KMNDMDFGDE GFEDAPF
//
