ID A5FP28_FLAJ1 Unreviewed; 475 AA. AC A5FP28; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 02-SEP-2026, entry version 113. DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|NCBIfam:TIGR00362}; GN Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377}; GN OrderedLocusNames=Fjoh_0005 {ECO:0000313|EMBL:ABQ03043.1}; OS Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / BCRC OS 14874 / CCUG 350202 / NBRC 14942 / NCIMB 11054 / UW101) (Cytophaga OS johnsonae). OC Bacteria; Pseudomonadati; Bacteroidota; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Flavobacterium. OX NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ03043.1, ECO:0000313|Proteomes:UP000006694}; RN [1] {ECO:0000313|EMBL:ABQ03043.1, ECO:0000313|Proteomes:UP000006694} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / BCRC 14874 / CCUG 350202 / RC NBRC 14942 / NCIMB 11054 / UW101 {ECO:0000313|Proteomes:UP000006694}; RX PubMed=19717629; DOI=10.1128/AEM.01495-09; RA McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G., RA Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R., RA Cheng Y.Q., Stein J.L.; RT "Novel features of the polysaccharide-digesting gliding bacterium RT Flavobacterium johnsoniae as revealed by genome sequence analysis."; RL Appl. Environ. Microbiol. 75:6864-6875(2009). 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:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}. CC -!- SUBUNIT: Oligomerizes as a right-handed, spiral filament on DNA at CC oriC. {ECO:0000256|HAMAP-Rule:MF_00377}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|HAMAP-Rule:MF_00377}. CC -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583, CC ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-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; CP000685; ABQ03043.1; -; Genomic_DNA. DR RefSeq; WP_011921525.1; NC_009441.1. DR AlphaFoldDB; A5FP28; -. DR STRING; 376686.Fjoh_0005; -. DR GeneID; 31762856; -. DR KEGG; fjo:Fjoh_0005; -. DR eggNOG; COG0593; Bacteria. DR HOGENOM; CLU_026910_3_0_10; -. DR OrthoDB; 9807019at2; -. DR Proteomes; UP000006694; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule. DR GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule. 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; 3.40.50.300:FF:000668; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00377}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_00377}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP- KW Rule:MF_00377}; KW Lipid-binding {ECO:0000256|ARBA:ARBA00023121, ECO:0000256|HAMAP- KW Rule:MF_00377}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00377}; Reference proteome {ECO:0000313|Proteomes:UP000006694}. FT DOMAIN 172..302 FT /note="AAA+ ATPase" FT /evidence="ECO:0000259|SMART:SM00382" FT DOMAIN 383..452 FT /note="Chromosomal replication initiator DnaA C-terminal" FT /evidence="ECO:0000259|SMART:SM00760" FT REGION 1..86 FT /note="Domain I, interacts with DnaA modulators" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" FT REGION 356..475 FT /note="Domain IV, binds dsDNA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" FT BINDING 183 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" FT BINDING 185 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" FT BINDING 186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" FT BINDING 187 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00377" SQ SEQUENCE 475 AA; 54506 MW; 4E6D59E6B85248A3 CRC64; MTKTAQSVWE NCLSFIKDNI QDQAYKTWFE PIKSVELTDN ALYIQVPSKF FYEWLEEHYV KLLKVALTKE LGKNAKLLYK IKMENTYGNK QPFTEQLPSS NRVPMKPQEV DAPFKNLNPE LKNPFVIPGI RNLKIESQLN PNYSFDNFLE GDSNRLARSA GMAVANKPGG TSFNPLLIFG GVGLGKTHLA HAIGVEVKDK YPEKTVLYIS AEIFTQQYID SVKKNNRNDF IHFYQLIDVL IIDDVQFLSG KSGTQDVFFH IFNYLHQNGK QVILTSDKAP VDMQDIEQRL LSRFKWGLSA ELHQPDYETR ISILKNILYR DGVDMPEDIL EYVARNIKSN VRELEGAIIS LIAQSSFNKK EVTIELAKSV VEKFVKNVKR EISIDYIQKI VSDYFQLDIE TLQSKTRKRH VVQARQLAMF FAKKFTKASL ANIGSQIGDR DHATVLHACK TVDNLVSTDK QFKKFVEDIN KKLTL //