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Database: UniProt
Entry: D5DUQ8_BACMQ
LinkDB: D5DUQ8_BACMQ
Original site: D5DUQ8_BACMQ 
ID   D5DUQ8_BACMQ            Unreviewed;       447 AA.
AC   D5DUQ8;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   05-JUL-2017, entry version 53.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ADE67142.1};
GN   OrderedLocusNames=BMQ_0001 {ECO:0000313|EMBL:ADE67142.1};
OS   Bacillus megaterium (strain ATCC 12872 / QMB1551).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=545693 {ECO:0000313|EMBL:ADE67142.1, ECO:0000313|Proteomes:UP000000935};
RN   [1] {ECO:0000313|Proteomes:UP000000935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12872 / QMB1551 {ECO:0000313|Proteomes:UP000000935};
RA   Eppinger M., Bunk B., Johns M.A., Edirisinghe J.N., Kutumbaka K.K.,
RA   Riley D.R., Creasy H.H., Koenig S.S.K., Galens K., Orvis J.,
RA   Creasy T., Biedendieck R., Braun C., Grayburn S., Jahn D., Ravel J.,
RA   Vary P.S.;
RT   "Genome sequences of the industrial vitamin B12-producers B.
RT   megaterium QM B1551 and DSM319 reveal new insights into the Bacillus
RT   genome evolution and pan-genome structure.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the initiation and regulation
CC       of chromosomal replication. Binds to the origin of replication; it
CC       binds specifically double-stranded DNA at a 9 bp consensus (dnaA
CC       box): 5'-TTATC[CA]A[CA]A-3'. DnaA binds to ATP and to acidic
CC       phospholipids. {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
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DR   EMBL; CP001983; ADE67142.1; -; Genomic_DNA.
DR   RefSeq; WP_013054820.1; NC_014019.1.
DR   STRING; 545693.BMQ_0001; -.
DR   EnsemblBacteria; ADE67142; ADE67142; BMQ_0001.
DR   KEGG; bmq:BMQ_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000935; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
DR   CDD; cd06571; Bac_DnaA_C; 1.
DR   Gene3D; 1.10.1750.10; -; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000935};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000935}.
FT   DOMAIN      143    271       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    424       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     151    158       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50823 MW;  EC4E47868E1B6FA6 CRC64;
     MENIHDLWDR ALDQIEKKLS KPSFETWLKS TKAHALQGDT LIITAPNDFA RDWLESRYSN
     LIAETLYDLT GEELDVKFII PPNQAEEEFD IQTPKKKVNK DEGAEFPQSM LNSKYTFDTF
     VIGSGNRFAH AASLAVAEAP AKAYNPLFIY GGVGLGKTHL MHAIGHYVLD HNPAAKVVYL
     SSEKFTNEFI NSIRDNKAVE FRNKYRNVDV LLIDDIQFLA GKEQTQEEFF HTFNTLHEES
     KQIVISSDRP PKEIPTLEDR LRSRFEWGLI TDITPPDLET RIAILRKKAK ADGLVIPNEV
     MLYIANQIDS NIRELEGALI RVVAYSSLIN KDINADLAAE ALKDIIPSSK PRVITIQDIQ
     QIVGQEFNIK LDDFKAKKRT KSVAFPRQIA MYLSRELTDF SLPKIGEEFG GRDHTTVIHA
     HEKISKLVQT DTDLQKQIKE ISESLKI
//
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