DNAA_DEIDV
ID DNAA_DEIDV Reviewed; 456 AA.
AC C1CXJ1;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 2.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377}; OrderedLocusNames=Deide_00010;
OS Deinococcus deserti (strain DSM 17065 / CIP 109153 / LMG 22923 / VCD115).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=546414;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17065 / CIP 109153 / LMG 22923 / VCD115;
RX PubMed=19370165; DOI=10.1371/journal.pgen.1000434;
RA de Groot A., Dulermo R., Ortet P., Blanchard L., Guerin P., Fernandez B.,
RA Vacherie B., Dossat C., Jolivet E., Siguier P., Chandler M., Barakat M.,
RA Dedieu A., Barbe V., Heulin T., Sommer S., Achouak W., Armengaud J.;
RT "Alliance of proteomics and genomics to unravel the specificities of Sahara
RT bacterium Deinococcus deserti.";
RL PLoS Genet. 5:E1000434-E1000434(2009).
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; CP001114; ACO44797.2; -; Genomic_DNA.
DR RefSeq; WP_012691920.1; NC_012526.1.
DR AlphaFoldDB; C1CXJ1; -.
DR SMR; C1CXJ1; -.
DR STRING; 546414.Deide_00010; -.
DR PaxDb; C1CXJ1; -.
DR EnsemblBacteria; ACO44797; ACO44797; Deide_00010.
DR KEGG; ddr:Deide_00010; -.
DR eggNOG; COG0593; Bacteria.
DR HOGENOM; CLU_026910_3_1_0; -.
DR OrthoDB; 219876at2; -.
DR Proteomes; UP000002208; 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; IPR024633; DnaA_N_dom.
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 Pfam; PF11638; DnaA_N; 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..456
FT /note="Chromosomal replication initiator protein DnaA"
FT /id="PRO_1000205649"
FT REGION 89..112
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..110
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 154..161
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ SEQUENCE 456 AA; 51482 MW; E50F45A06AEA464B CRC64;
MSQEIWADVL GYVRKNISEV EYHTWFAPLK NLGVQDGSLV LGVRNSFAQE WLRKQYQGLL
EDALRSLGAQ HPQVSFQVLP ASQDALLLPS DPPPAPISPG RAPAPPPADN RKTLNPKYTF
ENFVVGPNNN LAHAAALAVA ESPGKAYNPL FIYGDVGLGK THLMHAVGHY IAERFPEKRI
EYVSTETFTN ELINAIREDK TTQFRNRYRS VDLLLVDDIQ FLAGKERTQE EFFHTFNALY
ENHKQIILSS DRPPKDIQTL EGRLRSRFEW GLITDIQSPE FETRVAILKM NAEHNRIDIP
QEVLELIARQ VTTNIRELEG ALMRVVAFSS LNNVPFSRAV ASKALSNVFA PQEVKVEMMD
VLRQVASHFN MPPDVIRGSG RVREVVVPRQ VAQYLIRDLT DHSLPEIGQF FGRDHSTVMH
AISKVTEQLG KDSELTAAVE TLRRKMKGLE DEDSRA