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Database: UniProt
Entry: W0P5G9_9BURK
LinkDB: W0P5G9_9BURK
Original site: W0P5G9_9BURK 
ID   W0P5G9_9BURK            Unreviewed;       510 AA.
AC   W0P5G9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   05-JUL-2017, entry version 27.
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:AHG62104.1};
GN   ORFNames=MIM_c00010 {ECO:0000313|EMBL:AHG62104.1};
OS   Advenella mimigardefordensis DPN7.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae.
OX   NCBI_TaxID=1247726 {ECO:0000313|EMBL:AHG62104.1, ECO:0000313|Proteomes:UP000019095};
RN   [1] {ECO:0000313|EMBL:AHG62104.1, ECO:0000313|Proteomes:UP000019095}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPN7 {ECO:0000313|EMBL:AHG62104.1,
RC   ECO:0000313|Proteomes:UP000019095};
RX   PubMed=24739217; DOI=10.1099/mic.0.078279-0;
RA   Wubbeler J.H., Hiessl S., Schuldes J., Thurmer A., Daniel R.,
RA   Steinbuchel A.;
RT   "Unravelling the complete genome sequence of Advenella
RT   mimigardefordensis strain DPN7T and novel insights in the catabolism
RT   of the xenobiotic polythioester precursor 3,3'-dithiodipropionate.";
RL   Microbiology 160:1401-1416(2014).
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; CP003915; AHG62104.1; -; Genomic_DNA.
DR   RefSeq; WP_025370698.1; NZ_CP003915.1.
DR   EnsemblBacteria; AHG62104; AHG62104; MIM_c00010.
DR   KEGG; amim:MIM_c00010; -.
DR   PATRIC; fig|1247726.3.peg.2; -.
DR   KO; K02313; -.
DR   Proteomes; UP000019095; 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:UP000019095};
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:UP000019095}.
FT   DOMAIN      205    336       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      418    487       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     213    220       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   510 AA;  57275 MW;  DBAF9E3B688AFD74 CRC64;
     MQEFWQSCVH SLAQELPPEQ MKAWVHPLSF LSFDEELGEV RVSAPNAIKQ NWARTNYTQR
     IQELASNWFN RPGIRVIFQV ARRDQHHVSQ VHGPAVAPPA GMPAVAPAGA PAPREYTNGS
     VQPNGHGASA ALHTAARATA VVEPAVTGKE PTVVIETVGQ APEDHVYKRS HMNANLTFES
     LVIGKSNQLA NAASAQIVEN PGVSSYNPFF LYGSTGLGKT HLMHAIGNAL FKAGKVSRVR
     YIHADQYYSD MVKSFQTNTF DDLKRYYHSL DLLLIDDIQF FRKKERTQEE FFLLYETMVQ
     RGRQIVITSD TYPRELQDIN SRLTSRFDSG LTVQIEPPEL EMRVAILLRK AEEKTSIVLK
     EEAAFFIAKH LRSNVRELEG ALSRVSAYAG FHGVKIITVE FCKEALKDLL SVSIGQITIE
     NIQKTVADFY KLKVQEMYSK RRPANIAMAR QIAMYLAKEL TQKSLPEIGD SFGGRDHTTV
     LHAVRKITEQ RAKNAELNHQ LHVLEQTLKG
//
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