ID   DNAA_KINRD              Reviewed;         518 AA.
AC   A6W3V4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=Krad_0001;
OS   Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC   Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX   NCBI_TaxID=266940;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX   PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA   Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA   Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT   "Survival in nuclear waste, extreme resistance, and potential applications
RT   gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL   PLoS ONE 3:e3878-e3878(2008).
CC   -!- FUNCTION: Plays an important role in the initiation and regulation of
CC       chromosomal replication. Binds to the origin of replication; it binds
CC       specifically double-stranded DNA at a 9 bp consensus (dnaA box): 5'-
CC       TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic phospholipids.
CC       {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {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; CP000750; ABS01493.1; -; Genomic_DNA.
DR   RefSeq; WP_012085692.1; NC_009664.2.
DR   AlphaFoldDB; A6W3V4; -.
DR   SMR; A6W3V4; -.
DR   STRING; 266940.Krad_0001; -.
DR   EnsemblBacteria; ABS01493; ABS01493; Krad_0001.
DR   KEGG; kra:Krad_0001; -.
DR   eggNOG; COG0593; Bacteria.
DR   HOGENOM; CLU_026910_2_0_11; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   Proteomes; UP000001116; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 1.
DR   Gene3D; 3.30.300.180; -; 1.
DR   Gene3D; 3.40.50.300; -; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR038454; DnaA_N_sf.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF08299; Bac_DnaA_C; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00760; Bac_DnaA_C; 1.
DR   SUPFAM; SSF48295; SSF48295; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
DR   PROSITE; PS01008; DNAA; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; DNA replication; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..518
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000079952"
FT   REGION          91..174
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         218..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   518 AA;  57769 MW;  FDEF60367CC16025 CRC64;
     METDGGDFPS VWERALAQLD DGVTQHQRAF VRLTRPLGLL DGTALLAVPN DLTKDVIEQK
     VREPLTRALS EAYGSPIRLA VTVDPSIGQV LTPERTGEHS GGVGSVPSVE RERGSVLTGL
     DGDDGLHLDE RRSGSLEEDS PLDDSDPDLL FTGYKVDRGP GTGRQPRRPT TRIENSRLNP
     KYIFETFVIG ASNRFAHAAA VAVAEAPAKA YNPLFIYGES GLGKTHLLHA IGHYAQNLYP
     GVQVRYVNSE EFTNDFINSI RDDKAQAFQR RHRDVDVLLI DDIQFLSNKV QTQEEFFHTF
     NTLHNASKQV VITSDLPPKQ LSGFEERMRS RFEWGLITDV QPPDLETRIA ILRKKAIGER
     LEVPDDVNEY IASKISSNIR ELEGALIRVT AFASLNRQPV DMQLAEIVLR DLIPNEETPE
     ITAAAIMGQT ASYFSVTLED LCGTSRSRTL VTARQIAMYL CRELTELSLP KIGQHFGGRD
     HTTVMHAERK IKQQMAERRS TYNQVTELTN RIKKQSGA