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Database: UniProt
Entry: Q3JXI6
LinkDB: Q3JXI6
Original site: Q3JXI6 
ID   DNAA_BURP1              Reviewed;         533 AA.
AC   Q3JXI6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=BURPS1710b_0301;
OS   Burkholderia pseudomallei (strain 1710b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=320372;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1710b;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000124; ABA49564.1; -; Genomic_DNA.
DR   RefSeq; WP_004525818.1; NC_007434.1.
DR   AlphaFoldDB; Q3JXI6; -.
DR   SMR; Q3JXI6; -.
DR   EnsemblBacteria; ABA49564; ABA49564; BURPS1710b_0301.
DR   KEGG; bpm:BURPS1710b_0301; -.
DR   HOGENOM; CLU_026910_0_1_4; -.
DR   Proteomes; UP000002700; Chromosome I.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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   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; 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   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; Nucleotide-binding.
FT   CHAIN           1..533
FT                   /note="Chromosomal replication initiator protein DnaA"
FT                   /id="PRO_1000048619"
FT   REGION          83..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..112
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         238..245
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   533 AA;  58352 MW;  AC277CE737A21B6D CRC64;
     MNDFWQHCSA LLERELTPQQ YVTWIKPLAP VAFDAAANTL SIAAPNRFKL DWVKSQFSGR
     ISDLARDFWN APIEVQFVLD PKAGQRSPAG ATPLAPRAPL PSANPAPVAP GPASAPAVDA
     HAPAPAGMNA ATAAAVAAAQ AAQAAQANAA ALNADEAADL DLPSLTAHEA AAGRRTWRPG
     AANANSEAAD SMYERSKLNP VLTFDNFVTG KANQLARAAA IQVADNPGIS YNPLFLYGGV
     GLGKTHLIHA IGNQLLLDKP GARIRYIHAE QYVSDVVKAY QRKAFDDFKR YYHSLDLLLI
     DDIQFFSGKS RTQEEFFYAF EALVANKAQV IITSDTYPKE ISGIDDRLIS RFDSGLTVAI
     EPPELEMRVA ILMRKAQSEG VSLSEDVAFF VAKHLRSNVR ELEGALRKIL AYSKFHGREI
     TIELTKEALK DLLTVQNRQI SVENIQKTVA DFYNIKVADM YSKKRPANIA RPRQIAMYLA
     KELTQKSLPE IGELFGGRDH TTVLHAVRKI ADERGKDAQL NHELHVLEQT LKG
//
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