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Database: UniProt
Entry: A0A0D5LCB1_9BURK
LinkDB: A0A0D5LCB1_9BURK
Original site: A0A0D5LCB1_9BURK 
ID   A0A0D5LCB1_9BURK        Unreviewed;       530 AA.
AC   A0A0D5LCB1;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 29.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AJY41284.1};
GN   ORFNames=BW21_120 {ECO:0000313|EMBL:AJY41284.1};
OS   Burkholderia sp. 2002721687.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1468409 {ECO:0000313|EMBL:AJY41284.1, ECO:0000313|Proteomes:UP000032645};
RN   [1] {ECO:0000313|EMBL:AJY41284.1, ECO:0000313|Proteomes:UP000032645}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2002721687 {ECO:0000313|EMBL:AJY41284.1,
RC   ECO:0000313|Proteomes:UP000032645};
RX   PubMed=25931592;
RA   Johnson S.L., Bishop-Lilly K.A., Ladner J.T., Daligault H.,
RA   Jaissle J., Frey K.G., Koroleva G.I., Bruce D.C., Coyne S.R.,
RA   Broomall S.M., Li P., Teshima H., Gibbons H.S., Palacios G.F.,
RA   Rosenzweig C.N., McMurry K., Redden C.L., Xu Y., Currie B., Mayo M.,
RA   Minogue T.D., Chain P.S.;
RT   "Complete genome sequences for 59 burkholderia isolates, both
RT   pathogenic and near neighbor.";
RL   Genome Announc. 3:0-0(2015).
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; CP009549; AJY41284.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJY41284; AJY41284; BW21_120.
DR   KEGG; bul:BW21_120; -.
DR   PATRIC; fig|1468409.3.peg.135; -.
DR   KO; K02313; -.
DR   Proteomes; UP000032645; Chromosome I.
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   Gene3D; 3.30.300.180; -; 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   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:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032645};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117}.
FT   DOMAIN      227    361       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      438    507       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     235    242       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   530 AA;  57968 MW;  1E89A4C171433722 CRC64;
     MNDFWQHCSA LLERELTPQQ YVTWIKPLAP VAFDAAANTL SIAAPNRFKL DWVKSQFSGR
     ISDLARDFWN APIDVQFVLD PKAGQRSAAG TAPLAPRAPL SAANPAPVTA GPVPAGAVDA
     NAPAPAGMNA ATAAAVAAAQ AAKANAAALN ADEAADLDLP SLTAHEAAAG RRTWRPGAAS
     ANSEAADSMY ERSKLNPVLT FDNFVTGKAN QLARAAAIQV ADNPGISYNP LFLYGGVGLG
     KTHLIHAIGN QLLLDKPGAR IRYIHAEQYV SDVVKAYQRK AFDDFKRYYH SLDLLLIDDI
     QFFSGKSRTQ EEFFYAFEAL VANKAQVIIT SDTYPKEISG IDDRLISRFD SGLTVAIEPP
     ELEMRVAILM RKAQSEGVSL SEDVAFFVAK HLRSNVRELE GALRKILAYS KFHGREITIE
     LTKEALKDLL TVQNRQISVE NIQKTVADFY NIKVADMYSK KRPANIARPR QIAMYLAKEL
     TQKSLPEIGE LFGGRDHTTV LHAVRKIADE RGKDAQLNHE LHVLEQTLKG
//
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