ID   DNAA_AERHH              Reviewed;         456 AA.
AC   A0KEC3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   04-NOV-2026, entry version 110.
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=AHA_0001;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Aeromonadales; Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049;
RX   PubMed=16980456; DOI=10.1128/jb.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.H.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK36302.1; -; Genomic_DNA.
DR   RefSeq; WP_005307141.1; NC_008570.1.
DR   AlphaFoldDB; A0KEC3; -.
DR   SMR; A0KEC3; -.
DR   STRING; 380703.AHA_0001; -.
DR   PaxDb; 380703-AHA_0001; -.
DR   EnsemblBacteria; ABK36302; ABK36302; AHA_0001.
DR   GeneID; 4490513; -.
DR   GeneID; 47843307; -.
DR   KEGG; aha:AHA_0001; -.
DR   PATRIC; fig|380703.7.peg.2; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_0_1_6; -.
DR   OMA; AACMKFD; -.
DR   OrthoDB; 9807019at2; -.
DR   PRO; PR:A0KEC3; -.
DR   Proteomes; UP000000756; 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; 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; 3.30.300.180:FF:000001; 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..456
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000048599"
FT   REGION          1..83
FT                   /note="Domain I, interacts with DnaA modulators"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          83..119
FT                   /note="Domain II"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          92..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..336
FT                   /note="Domain III, AAA+ region"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   REGION          337..456
FT                   /note="Domain IV, binds dsDNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   COMPBIAS        105..117
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         164
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         166
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         167
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
FT   BINDING         168
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   456 AA;  51865 MW;  ECFA28DC67A0CD8D CRC64;
     MTASLWQQCL NRLQDELPSA EFSMWIRPLQ AELSDNTLTL YAPNRFVLDW VRDKYLIRVN
     GIINELCGVD GPTLRFDIGN RPHPVAVARA PARGADPVNN SQKSWESKAE AKPEPNHKSN
     TNVNYTFENF VEGKSNQLAR AAARQVADNP GGAYNPLFLY GGTGLGKTHL LHAVGNAIKE
     RKQDAKVIYM HSERFVQDMV KALQNNAIEE FKRYYRSVDA LLIDDIQFFA NKERSQEEFF
     HTFNALLEGN QQIILTSDRY PKEINGVEDR LKSRFGWGLT VAIEPPELET RVAILMRKAD
     ENQIHLPDEV AFFIAKRLRS NVRELEGALN RVIANANFTG RAINIDFVRE ALRDLLALQE
     KLVTIDNIQK TVAEYYKIKL ADLLSKRRSR SVARPRQLAM ALAKELTNHS LPEIGDAFGG
     RDHTTVLHAC RKIEQLKEES HDIKEDYSNL IRTLSS
//