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Database: UniProt
Entry: D4G385_BACNB
LinkDB: D4G385_BACNB
Original site: D4G385_BACNB 
ID   D4G385_BACNB            Unreviewed;       446 AA.
AC   D4G385;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 76.
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   ECO:0000313|EMBL:BAI83445.1};
GN   ORFNames=BSNT_00001 {ECO:0000313|EMBL:BAI83445.1};
OS   Bacillus subtilis subsp. natto (strain BEST195).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=645657 {ECO:0000313|EMBL:BAI83445.1, ECO:0000313|Proteomes:UP000006805};
RN   [1] {ECO:0000313|EMBL:BAI83445.1, ECO:0000313|Proteomes:UP000006805}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI83445.1,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=20398357; DOI=10.1186/1471-2164-11-243;
RA   Nishito Y., Osana Y., Hachiya T., Popendorf K., Toyoda A., Fujiyama A.,
RA   Itaya M., Sakakibara Y.;
RT   "Whole genome assembly of a natto production strain Bacillus subtilis natto
RT   from very short read data.";
RL   BMC Genomics 11:243-243(2010).
RN   [2] {ECO:0000313|EMBL:BAI83445.1, ECO:0000313|Proteomes:UP000006805}
RP   GENOME REANNOTATION.
RC   STRAIN=BEST195 {ECO:0000313|EMBL:BAI83445.1,
RC   ECO:0000313|Proteomes:UP000006805};
RX   PubMed=25329997; DOI=10.1371/journal.pone.0109999;
RA   Kamada M., Hase S., Sato K., Toyoda A., Fujiyama A., Sakakibara Y.;
RT   "Whole genome complete resequencing of Bacillus subtilis natto by combining
RT   long reads with high-quality short reads.";
RL   PLoS ONE 9:E109999-E109999(2014).
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; AP011541; BAI83445.1; -; Genomic_DNA.
DR   RefSeq; WP_003242674.1; NC_017196.2.
DR   AlphaFoldDB; D4G385; -.
DR   SMR; D4G385; -.
DR   STRING; 86029.AWV81_00005; -.
DR   GeneID; 83883200; -.
DR   KEGG; bso:BSNT_00001; -.
DR   PATRIC; fig|645657.3.peg.1; -.
DR   HOGENOM; CLU_026910_3_1_9; -.
DR   Proteomes; UP000006805; Chromosome.
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          143..271
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          355..424
FT                   /note="Chromosomal replication initiator DnaA C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00760"
FT   BINDING         151..158
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00377"
SQ   SEQUENCE   446 AA;  50859 MW;  666799A0A183C992 CRC64;
     MENILDLWNQ ALAQIEKKLS KPSFETWMKS TKAHSLQGDT LTITAPNEFA RDWLESRYLH
     LIADTIYELT GEELSIKFVI PQNQDVEDFM PKPQVKKAVK EDTSDFPQNM LNPKYTFDTF
     VIGSGNRFAH AASLAVAEAP AKAYNPLFIY GGVGLGKTHL MHAIGHYVID HNPSAKVVYL
     SSEKFTNEFI NSIRDNKAVD FRNRYRNVDV LLIDDIQFLA GKEQTQEEFF HTFNTLHEES
     KQIVISSDRP PKEIPTLEDR LRSRFEWGLI TDITPPDLET RIAILRKKAK AEGLDIPNEV
     MLYIANQIDS NIRELEGALI RVVAYSSLIN KDINADLAAE ALKDIIPSSK PKVITIKEIQ
     RVVGQQFNIK LEDFKAKKRT KSVAFPRQIA MYLSREMTDS SLPKIGEEFG GRDHTTVIHA
     HEKISKLLAD DEQLQQHVKE IKEQLK
//
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