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Database: UniProt
Entry: A0A0D3LAW1_9BACT
LinkDB: A0A0D3LAW1_9BACT
Original site: A0A0D3LAW1_9BACT 
ID   A0A0D3LAW1_9BACT        Unreviewed;       508 AA.
AC   A0A0D3LAW1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=D770_03610 {ECO:0000313|EMBL:AHM58989.1};
OS   Flammeovirgaceae bacterium 311.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Flammeovirgaceae.
OX   NCBI_TaxID=1257021 {ECO:0000313|EMBL:AHM58989.1, ECO:0000313|Proteomes:UP000064112};
RN   [1] {ECO:0000313|EMBL:AHM58989.1, ECO:0000313|Proteomes:UP000064112}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=311 {ECO:0000313|EMBL:AHM58989.1,
RC   ECO:0000313|Proteomes:UP000064112};
RA   Fang C.;
RT   "Complete bacteria genome obtained just from illumina data.";
RL   Submitted (NOV-2012) 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}.
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DR   EMBL; CP004371; AHM58989.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0D3LAW1; -.
DR   STRING; 1257021.D770_03610; -.
DR   KEGG; fbt:D770_03610; -.
DR   PATRIC; fig|1257021.3.peg.830; -.
DR   Proteomes; UP000064112; Chromosome.
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:AHM58989.1};
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:UP000064112}.
FT   DOMAIN          174..449
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          475..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   508 AA;  55974 MW;  F7A2A77A2095600B CRC64;
     MGKMPPQAID LEEAVLGALM LEKEAITTVI DILKTDNFYR EQHKLIYEAI IDLFNASEPV
     DLLTVSNQLR KNGTLDKVGG AFYITNLTTR VNSAANIEYH ARIVAEMAIK RKLITIAGEI
     QREAYEDTAD VFDLLDKTES ALFEVSEANI RKNYADMKTI MRDAMRELEA RKDHKDGLTG
     VPSGFSALDR VTSGWQPSDL IIIAARPAMG KTAFVVSALR NAAVDFNKPV AIFSLEMSAV
     QLVNRMISAE AELESEKIKK GNLADYEWEQ LVHKTTRLNK APIFIDDTPA LSVLELRAKC
     RRLKAQHDIQ MIIIDYLQLM SGDTSKGGGK GNREQEIASI SRALKQLAKE LNCPVIALSQ
     LSRAVETRGG DKRPQLSDLR ESGSIEQDAD MVMFLYRPEY YGILQGENGE PLAGVGEVII
     AKHRNGSLDT VQLKFIGKYT RFTDLDGPSI SNSNYAPSGN FTPVKTMSGG NVNSITLGSK
     ANDDDLSPKP GKPGFGYTDF PEDDGAPF
//
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