DNAB_RICTY
ID DNAB_RICTY Reviewed; 497 AA.
AC Q68WJ2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Replicative DNA helicase;
DE EC=3.6.4.12;
GN Name=dnaB; OrderedLocusNames=RT0531;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AE017197; AAU04000.1; -; Genomic_DNA.
DR RefSeq; WP_011190981.1; NC_006142.1.
DR AlphaFoldDB; Q68WJ2; -.
DR SMR; Q68WJ2; -.
DR STRING; 257363.RT0531; -.
DR EnsemblBacteria; AAU04000; AAU04000; RT0531.
DR KEGG; rty:RT0531; -.
DR eggNOG; COG0305; Bacteria.
DR HOGENOM; CLU_005373_0_2_5; -.
DR OMA; IEFHARI; -.
DR OrthoDB; 1709134at2; -.
DR Proteomes; UP000000604; 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..497
FT /note="Replicative DNA helicase"
FT /id="PRO_0000281068"
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 497 AA; 56194 MW; BC7826600862D76E CRC64;
MVRNKINNNI NIITNNDDNL SIPRVLPSNI QAEQMLLGAI ITNNELLSYV SEFLRNEHFF
EPIHQKIYDA IEKIIEKGLI ATPITLRSML TQDALFQEIE GVEYLAKLIT MSMMVINPID
YGKIIYDLAI KRNLINIGEE VVNNAYNASL AVAAKEQIEH AEAKLYDLAR EGLNEKSFTQ
VGISIAESLA SINKAMKNND HVIGISTGLL DLDNKLFGFH NSDLIILAGR PSMGKTAFAI
NLALNTCNNM RLKNIRDNQE IKSVGFFSLE MSSEQLTTRL LSLCAEIDST SLRTGMLSEE
KYNRLRKEAN TLSELQFFID DTPALSISAI RTRARRMKRK HNLGILFIDY LQLIRGVSKS
ENRVNEISEI TQGLKAIAKE LNIPVIALSQ LSRAVELRED KKPMLSDLRE SGTIEQDADI
VMFIYREEYY LTRKEPAAGD AKHAEWLDKL NKVYNIADII IAKHRNGPVG NISLYYDSQF
SKFGNLEKRT FNSILNT