DNAB_RICCN
ID DNAB_RICCN Reviewed; 494 AA.
AC Q92HG8;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=RC0803;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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:0000250}.
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 -!- SIMILARITY: Belongs to the helicase family. DnaB subfamily.
CC {ECO:0000305}.
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DR EMBL; AE006914; AAL03341.1; -; Genomic_DNA.
DR PIR; C97800; C97800.
DR RefSeq; WP_004998193.1; NC_003103.1.
DR AlphaFoldDB; Q92HG8; -.
DR SMR; Q92HG8; -.
DR EnsemblBacteria; AAL03341; AAL03341; RC0803.
DR KEGG; rco:RC0803; -.
DR HOGENOM; CLU_005373_0_2_5; -.
DR OMA; IEFHARI; -.
DR Proteomes; UP000000816; Chromosome.
DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0006269; P:DNA replication, synthesis of RNA primer; IEA:UniProtKB-KW.
DR CDD; cd00984; DnaB_C; 1.
DR Gene3D; 1.10.860.10; -; 1.
DR Gene3D; 3.40.50.300; -; 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 Pfam; PF00772; DnaB; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR SUPFAM; SSF48024; SSF48024; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00665; DnaB; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA replication; DNA-binding; Helicase; Hydrolase;
KW Nucleotide-binding; Primosome.
FT CHAIN 1..494
FT /note="Replicative DNA helicase"
FT /id="PRO_0000102028"
FT DOMAIN 198..490
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
FT BINDING 229..236
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00596"
SQ SEQUENCE 494 AA; 55756 MW; B7B37D3F371FA779 CRC64;
MARNKINNET NILADNEDNL PIPRVLPSNV QAEQMLLGAI LTNNELLNYV SEFLRDEHFF
EPIHQKIYKA IEKITEKGLT ATPITLRSML TQDELFQEVE GAEYLAKLIT MSMMVINPLD
YGKIIYDLAI KRNLINIGEE VVNNAYNSSL EVEAKEQIEH AEAKLYDLAS EGLNEKSFTK
IGISISESLA SINRAMKNND HIIGISTGLI DLDNKLCGFH NSDLIILAGR PSMGKTAFAI
NLALNACNNM RLKNIRDNQE IQSVGFFSLE MSSEQLTTRL LSMCAEIDST SLRTGILGEE
KYNRLRKEAN TLSELQFFID DTPALSISAI RTRARRMKRK HNLGILFIDY LQLIRGVSKS
ENRVSEISEI TQGLKAIAKE LNIPVIALSQ LSRAVELRED KKPMLSDLRE SGTIEQDADI
VMFIYREEYY LTRKEPAAGD AKHAAWLDKL NKVYNIADII VAKHRNGPVG NVPLYYDSQF
SKFGNLETRT FNSN