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Database: UniProt
Entry: A0A098G684_9GAMM
LinkDB: A0A098G684_9GAMM
Original site: A0A098G684_9GAMM 
ID   A0A098G684_9GAMM        Unreviewed;       460 AA.
AC   A0A098G684;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:CEG57479.1};
GN   ORFNames=LFA_2094 {ECO:0000313|EMBL:CEG57479.1};
OS   Legionella fallonii LLAP-10.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG57479.1, ECO:0000313|Proteomes:UP000032430};
RN   [1] {ECO:0000313|Proteomes:UP000032430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA   Gomez-Valero L.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Participates in initiation and elongation during chromosome
CC       replication; it exhibits DNA-dependent ATPase activity and contains
CC       distinct active sites for ATP binding, DNA binding, and interaction
CC       with DnaC protein, primase, and other prepriming proteins.
CC       {ECO:0000256|ARBA:ARBA00003574, 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; LN614827; CEG57479.1; -; Genomic_DNA.
DR   RefSeq; WP_045095970.1; NZ_LN614827.1.
DR   AlphaFoldDB; A0A098G684; -.
DR   STRING; 1212491.LFA_2094; -.
DR   KEGG; lfa:LFA_2094; -.
DR   HOGENOM; CLU_005373_0_0_6; -.
DR   OrthoDB; 9773982at2; -.
DR   Proteomes; UP000032430; 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: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|ARBA:ARBA00022806, ECO:0000256|RuleBase:RU362085};
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:UP000032430}.
FT   DOMAIN          188..455
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  50577 MW;  F48D1402705B73DC CRC64;
     MLDLQSAKKT VDPLKRPPHS AEAEQSIIGG LMLDNQVWDK ISTKLCEADF YRTEHKVLFK
     TIAALVKKEQ PFDVVTLLDA LKSHNELDDA GGEAYLFELA NNTPSVANVT AYADIVREKS
     VQRQLIAVAT EIADSAYNPS GREVPELLDF AETKVFAIGE QTGGDGGPEA IKSILVRTVE
     KIDQLYHSTD AITGLATGLS DLDEMTSGLQ PSDLVIVAGR PSMGKTTLVM NMAEHAAIKV
     NKPVLVFSME MPSDSLAMRM MSSLGRIDQH RIRTGKLDDD DWPRVTSAVH MLSEASLFID
     DTPALSPAEM RARARRLAKE HGALGLIVVD YLQLMKIPGF NAENRTAEIS EISRSLKSLA
     KELQVPVIAL SQLNRSLEQR ADKRPVMSDL RESGAIEQDA DLICFIYRDE VYNEDSPDKG
     TAEIIIAKQR NGPIGKVRVA FIGKYTRFED LAFSGYQGAD
//
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