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Database: UniProt
Entry: G4M740_9BURK
LinkDB: G4M740_9BURK
Original site: G4M740_9BURK 
ID   G4M740_9BURK            Unreviewed;       462 AA.
AC   G4M740;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
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=BKIR_c157_1334 {ECO:0000313|EMBL:CCD36967.1};
OS   Candidatus Paraburkholderia kirkii UZHbot1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1055526 {ECO:0000313|EMBL:CCD36967.1, ECO:0000313|Proteomes:UP000003511};
RN   [1] {ECO:0000313|EMBL:CCD36967.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD36967.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CCD36967.1, ECO:0000313|Proteomes:UP000003511}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot1 {ECO:0000313|EMBL:CCD36967.1,
RC   ECO:0000313|Proteomes:UP000003511};
RA   Carlier A.L., Eberl L.;
RT   "Draft genome sequence of Candidatus Burkholderia kirkii.";
RL   Submitted (OCT-2011) 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}.
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:CCD36967.1}.
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DR   EMBL; CAFE01000070; CCD36967.1; -; Genomic_DNA.
DR   AlphaFoldDB; G4M740; -.
DR   STRING; 1055526.BKIR_c157_1334; -.
DR   HOGENOM; CLU_005373_0_0_4; -.
DR   BioCyc; CBUR1055526:G10QW-1986-MONOMER; -.
DR   Proteomes; UP000003511; 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|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:UP000003511}.
FT   DOMAIN          190..456
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
SQ   SEQUENCE   462 AA;  50958 MW;  962E06C690CB618D CRC64;
     MNAPSKDPQL DALKVPPHSI EAEQSVLGGL LLDNAAWDRI ADVMARSDFY RYDHRIIYEH
     IGKLIAATRP ADVITVYEAL TMAGKAEEVG GLAYLNALAQ NTPSAANIRR YAEIVRDRAV
     LRRLVSVADE ISADAFNPQG KEVRQILDEA ESRVFSIAEE GARGTQGFLE IGPLLTQVVE
     RIDTLYHTAN PSDVTGTPTG FVDLDRMTSG MHGGELIIVA GRPSMGKTAF SMNIGEYVAV
     EYGLPVAVFS MEMPGTQLTM RMLGSVGRLD QHRMRTGRLT DEDWPKLTHA VQKMSEAQLF
     IDETGDLNPM ELRSRARRLS RQCGKLGLII VDYLQLMSGS GGGENRATEI SEISRSLKSL
     AKELDVPMIA LSQLNRGLEQ RPNKRPIMSD LRESGAIEQD ADVILFIYRD EVYNPDSPDK
     GTAEIIIGKQ RNGPIGPVRL TFHGQYTKFD NFACAQNFYG GE
//
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