ID DNAA_COXBU Reviewed; 451 AA. AC Q83FD8; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 02-SEP-2026, entry version 119. DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377}; GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; GN OrderedLocusNames=CBU_0001; OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Legionellales; Coxiellaceae; Coxiella. OX NCBI_TaxID=227377; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RSA 493 / Nine Mile phase I; RX PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C., RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T., RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M., RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E., RA Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). CC -!- FUNCTION: Plays an essential role in the initiation and regulation of CC chromosomal replication. ATP-DnaA binds to the origin of replication CC (oriC) to initiate formation of the DNA replication initiation complex CC once per cell cycle. Binds the DnaA box (a 9 base pair repeat at the CC origin) and separates the double-stranded (ds)DNA. Forms a right-handed CC helical filament on oriC DNA; dsDNA binds to the exterior of the CC filament while single-stranded (ss)DNA is stabiized in the filament's CC interior. The ATP-DnaA-oriC complex binds and stabilizes one strand of CC the AT-rich DNA unwinding element (DUE), permitting loading of DNA CC polymerase. After initiation quickly degrades to an ADP-DnaA complex CC that is not apt for DNA replication. Binds acidic phospholipids. CC {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- SUBUNIT: Oligomerizes as a right-handed, spiral filament on DNA at CC oriC. {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- DOMAIN: Domain I is involved in oligomerization and binding regulators, CC domain II is flexibile and of varying length in different bacteria, CC domain III forms the AAA+ region, while domain IV binds dsDNA. CC {ECO:0000255|HAMAP-Rule:MF_00377}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP- CC Rule:MF_00377}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE016828; AAO89571.1; -; Genomic_DNA. DR RefSeq; NP_819057.1; NC_002971.4. DR RefSeq; WP_005769932.1; NC_002971.4. DR AlphaFoldDB; Q83FD8; -. DR SMR; Q83FD8; -. DR STRING; 227377.CBU_0001; -. DR EnsemblBacteria; AAO89571; AAO89571; CBU_0001. DR GeneID; 1207921; -. DR KEGG; cbu:CBU_0001; -. DR PATRIC; fig|227377.7.peg.2; -. DR eggNOG; COG0593; Bacteria. DR HOGENOM; CLU_026910_0_1_6; -. DR OrthoDB; 9807019at2; -. DR Proteomes; UP000002671; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003688; F:DNA replication origin binding; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IBA:GO_Central. DR GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd00009; AAA; 1. DR CDD; cd06571; Bac_DnaA_C; 1. DR FunFam; 1.10.1750.10:FF:000001; Chromosomal replication initiator protein DnaA; 1. DR FunFam; 1.10.8.60:FF:000003; Chromosomal replication initiator protein DnaA; 1. DR FunFam; 3.40.50.300:FF:000103; Chromosomal replication initiator protein DnaA; 1. DR Gene3D; 1.10.1750.10; -; 1. DR Gene3D; 1.10.8.60; -; 1. DR Gene3D; 3.30.300.180; -; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00377; DnaA_bact; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001957; Chromosome_initiator_DnaA. DR InterPro; IPR020591; Chromosome_initiator_DnaA-like. DR InterPro; IPR018312; Chromosome_initiator_DnaA_CS. DR InterPro; IPR013159; DnaA_C. DR InterPro; IPR013317; DnaA_dom. DR InterPro; IPR024633; DnaA_N_dom. DR InterPro; IPR038454; DnaA_N_sf. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR010921; Trp_repressor/repl_initiator. DR NCBIfam; TIGR00362; DnaA; 1. DR PANTHER; PTHR30050; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1. DR PANTHER; PTHR30050:SF2; CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA; 1. DR Pfam; PF00308; Bac_DnaA; 1. DR Pfam; PF08299; Bac_DnaA_C; 1. DR Pfam; PF11638; DnaA_N; 1. DR PRINTS; PR00051; DNAA. DR SMART; SM00382; AAA; 1. DR SMART; SM00760; Bac_DnaA_C; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF48295; TrpR-like; 1. DR PROSITE; PS01008; DNAA; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; DNA replication; DNA-binding; Lipid-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..451 FT /note="Chromosomal replication initiator protein DnaA" FT /id="PRO_0000114170" FT REGION 1..72 FT /note="Domain I, interacts with DnaA modulators" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT REGION 72..114 FT /note="Domain II" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT REGION 81..106 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 115..331 FT /note="Domain III, AAA+ region" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT REGION 332..451 FT /note="Domain IV, binds dsDNA" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT COMPBIAS 81..90 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 159 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT BINDING 161 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT BINDING 162 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" FT BINDING 163 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377" SQ SEQUENCE 451 AA; 51096 MW; 4615CFBF16DE0C5E CRC64; MSLPTSLWDK CLGYLRDEIP PQQYNTWIRP LHAIESKQNG LLLLAPNRFV LDWINERFLN RITELLDELS DTPPQIRLQI GSRSTEMPTK NSHEPSHRKA AAPPAGTTIS HTQANINSNF TFDSFVEGKS NQLARAAATQ VAENPGQAYN PLFIYGGVGL GKTHLMHAVG NAILRKDSSK KVLYLHSERF VADMIKALQH NAMNEFKRFY RSLNALLIDD IQFFAGKDRS QEEFFHTFNA LLDGQQQIIL TCDRYPKEIN GLEERLQSRF GWGLTVAIEP PELETRVAIL MSKAEQLKVH LPHEVAFFIA KHIQSNVREL EGALKRVIAN AHFTGQSITV DFTREALKDL LTLQARLITI ENIQKTVAEY YKIKVADLLA KRRNRSVARP RQMAMALAKE LTNHSLPEIG DAFGGRDHTT VLHACRKVKE LLATSLDILE DYKNLMRILS G //