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Database: UniProt
Entry: I2DI96_9BURK
LinkDB: I2DI96_9BURK
Original site: I2DI96_9BURK 
ID   I2DI96_9BURK            Unreviewed;       525 AA.
AC   I2DI96;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|ARBA:ARBA00018893, ECO:0000256|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=MYA_0002 {ECO:0000313|EMBL:AFJ84372.1};
OS   Burkholderia sp. KJ006.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ84372.1, ECO:0000313|Proteomes:UP000010108};
RN   [1] {ECO:0000313|EMBL:AFJ84372.1, ECO:0000313|Proteomes:UP000010108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KJ006 {ECO:0000313|EMBL:AFJ84372.1,
RC   ECO:0000313|Proteomes:UP000010108};
RX   PubMed=22843575; DOI=10.1128/JB.00821-12;
RA   Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA   Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT   "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT   Strain KJ006.";
RL   J. Bacteriol. 194:4432-4433(2012).
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:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|ARBA:ARBA00006583,
CC       ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU004227}.
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DR   EMBL; CP003514; AFJ84372.1; -; Genomic_DNA.
DR   RefSeq; WP_011882715.1; NC_017920.1.
DR   AlphaFoldDB; I2DI96; -.
DR   SMR; I2DI96; -.
DR   KEGG; buk:MYA_0002; -.
DR   PATRIC; fig|416344.3.peg.2; -.
DR   HOGENOM; CLU_026910_0_1_4; -.
DR   Proteomes; UP000010108; Chromosome 1.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00377};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_00377};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00377}.
FT   DOMAIN          222..356
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          433..502
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   REGION          160..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         230..237
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   525 AA;  57776 MW;  B4AF90954EB78C66 CRC64;
     MNDFWQHCSA LLERELTPQQ YVTWIKPLAP VAFDASANTL SIAAPNRFKL DWVKSQFSGR
     IADLAREFWN TPIEVQFVLD PKAGMRGAPA GVAPAAPRMP LTPNGPAAAV AAIAANLTAH
     ASAAPSAPAD VPLTPSAAAA HHLHGDDADI DLPSLPAHEA AAGRRTWRPG PGAAPANGAE
     ADSMYERSKL NPVLTFDNFV TGKANQLARA AAIQVAHNPG ISYNPLFLYG GVGLGKTHLI
     HAIGNQLLLD KAGARIRYIH AEQYVSDVVK AYQRKAFDDF KRYYHSLDLL LIDDIQFFSG
     KSRTQEEFFY AFEALVANKA QVIITSDTYP KEISGIDDRL ISRFDSGLTV AIEPPELEMR
     VAILMRKAQS EGVNLSEDVA FFVAKHLRSN VRELEGALRK ILAYSKFHGR EISIELTKEA
     LKDLLTVQNR QISVENIQKT VADFYNIKVA DMYSKKRPAN IARPRQIAMY LAKELTQKSL
     PEIGELFGGR DHTTVLHAVR KIADERGKDA QLNHELHVLE QTLKG
//
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