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Database: UniProt
Entry: A0A0J7MHP6_9BURK
LinkDB: A0A0J7MHP6_9BURK
Original site: A0A0J7MHP6_9BURK 
ID   A0A0J7MHP6_9BURK        Unreviewed;       505 AA.
AC   A0A0J7MHP6;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ORFNames=BPMI_01056 {ECO:0000313|EMBL:KMQ80295.1};
OS   Candidatus Burkholderia pumila.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1090375 {ECO:0000313|EMBL:KMQ80295.1, ECO:0000313|Proteomes:UP000054273};
RN   [1] {ECO:0000313|EMBL:KMQ80295.1, ECO:0000313|Proteomes:UP000054273}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot3 {ECO:0000313|EMBL:KMQ80295.1,
RC   ECO:0000313|Proteomes:UP000054273};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) 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:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KMQ80295.1}.
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DR   EMBL; LELG01000115; KMQ80295.1; -; Genomic_DNA.
DR   EnsemblBacteria; KMQ80295; KMQ80295; BPMI_01056.
DR   PATRIC; fig|1090375.4.peg.511; -.
DR   Proteomes; UP000054273; Unassembled WGS sequence.
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   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: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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054273};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054273}.
FT   DOMAIN      202    336       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      413    482       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     210    217       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   505 AA;  55895 MW;  869FDEF40D200B06 CRC64;
     MNDFWKHCSA LLERELTPQQ YVTWIKPLTP VDFDAGANTL RIAAPNRFKL DWVKSQFSGR
     IADVAREFFG ANIDVQFVLD PKATARNAIG GGPATAPRPS APVVAQANAT AHINALAAEA
     AAQQAAAQAQ ATQDDQADLD LPSMDAQEAA AGRRTWRGGA PDSAYERSKL NPVLTFDNFV
     TGKANQLARA AAIQVADNPG ISYNPLFLYG GVGLGKTHLI HAIGNQLLMD KAGTRIRYIH
     AEQYVSDVVK AYQRKAFDDF KRYYHSLDLL LIDDIQFFSG KSRTQEEFFY AFEALVANKA
     QVIITSDTYP KEISGIDDRL ISRFDSGLTV AIEPPELEMR VAILMRKASS EGVSLSEDVA
     FFVAKHLRSN VRELEGALRK ILAYSKFHGR DITIELTKEA LKDLLTVQNR QISVENIQKT
     AADFYNIKVA DIYSKKRPAN IARPRQIAMY LAKELTQKSL PEIGELFGGR DHTTVLHAVR
     KIAAERGTDA QLNHELHVLE QTLKG
//
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