ID   DNAA_ROSCS              Reviewed;         480 AA.
AC   A7NFB8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   02-SEP-2026, entry version 98.
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=Rcas_0001;
OS   Roseiflexus castenholzii (strain DSM 13941 / HLO8).
OC   Bacteria; Bacillati; Chloroflexota; Chloroflexia; Chloroflexales;
OC   Roseiflexineae; Roseiflexaceae; Roseiflexus.
OX   NCBI_TaxID=383372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13941 / HLO8;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Bryant D.A., Hanada S., Tsukatani Y., Richardson P.;
RT   "Complete sequence of Roseiflexus castenholzii DSM 13941.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; CP000804; ABU56140.1; -; Genomic_DNA.
DR   RefSeq; WP_011997546.1; NC_009767.1.
DR   AlphaFoldDB; A7NFB8; -.
DR   SMR; A7NFB8; -.
DR   STRING; 383372.Rcas_0001; -.
DR   KEGG; rca:Rcas_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_3_1_0; -.
DR   OrthoDB; 9807019at2; -.
DR   Proteomes; UP000000263; 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:000150; 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..480
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000079959"
FT   REGION          1..71
FT                   /note="Domain I, interacts with DnaA modulators"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          71..139
FT                   /note="Domain II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          91..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..356
FT                   /note="Domain III, AAA+ region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          357..480
FT                   /note="Domain IV, binds dsDNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   COMPBIAS        97..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         186
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         188
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   480 AA;  54091 MW;  FF31B7DE6AF4D453 CRC64;
     MNLTKVWNTT LGSLQVQLPR HEYNTWVRGA NLLDIDNGVA IIRAPNAFIK EGLESRYLTT
     LREQLGSVVG FPVDVRIVLA TSESERIDGA SINGRHAARD TRKSDHHAPL SGGYGNGISH
     PLERASVHQL ELHRAVRSSM LNPRYTFDRF IIGPSNRLAN AACMAVAEHP AQAYNPLFLY
     GGVGLGKTHL LHAIGNFVLD RDPEVNVLYV SSETFTNDLI NSIRRQQTEE FRIRYRNIDI
     LLIDDIQFIA GKEQTQEEFF HTFNTLHSAG KQIIISSDRS PKAILTLEER LRSRFEWGLI
     VDVQMPDLET RTAILRAKAE QSPVPVPQPV IDFLAQRIQS HIRELEGCLN RVTAYAQMYN
     IPVTIEVATA ALSELLDTNR RKRVTPEAIL REVAAFYSVD LRSLQGRGRS RNIVTPRHVA
     MYLLREETDS SLMEIGQLLG GRDHTTVMYG CDKIAEEINT DARLRQEVAA IRERLMNSAV
//