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Database: UniProt
Entry: A0A109D0Y3_9BURK
LinkDB: A0A109D0Y3_9BURK
Original site: A0A109D0Y3_9BURK 
ID   A0A109D0Y3_9BURK        Unreviewed;       459 AA.
AC   A0A109D0Y3;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   25-OCT-2017, entry version 14.
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=APY03_2114 {ECO:0000313|EMBL:KWT96908.1};
OS   Variovorax sp. WDL1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=207745 {ECO:0000313|EMBL:KWT96908.1, ECO:0000313|Proteomes:UP000065640};
RN   [1] {ECO:0000313|EMBL:KWT96908.1, ECO:0000313|Proteomes:UP000065640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WDL1 {ECO:0000313|EMBL:KWT96908.1,
RC   ECO:0000313|Proteomes:UP000065640};
RA   Albers P.;
RT   "Transcriptomic analysis of a linuron degrading triple-species
RT   bacterial consortium.";
RL   Submitted (OCT-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:KWT96908.1}.
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DR   EMBL; LMTS01000076; KWT96908.1; -; Genomic_DNA.
DR   RefSeq; WP_068676675.1; NZ_LMTS01000076.1.
DR   EnsemblBacteria; KWT96908; KWT96908; APY03_2114.
DR   PATRIC; fig|207745.3.peg.7597; -.
DR   Proteomes; UP000065640; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000065640};
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:UP000065640}.
FT   DOMAIN      156    290       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     164    171       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      436    459       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   459 AA;  51597 MW;  883389C9E569FD92 CRC64;
     MPSEGIGDSL WQACVDQLAQ ELSEQQFNTW IKPLTARVAD DLSRVTVFVA NRFKLDWIRA
     QYAGKIAAMA EKLYGQPVII ELALAPREIV ARPVSMAVTF ETDVPRDVAG PGEDPSGGAF
     KNRLNSGLTF DTLVEGTANR MARAAAMHVA GMPGHLYNPL FIYGGVGLGK THLMHAVGNR
     LLSDRPDAKV LYIHAEQFVS DVVKAYQRKT FDEFKERYHS LDLLLIDDVQ FFANKDRTQE
     EFFNAFEALL AKKSHIVMTS DTYPKGLSDI HERLVSRFDS GLTVAIEPPE LEMRVAILIN
     KARAENAEMP EEVAFFVAKN VRSNVRELEG ALRKILAYSR FNQKEISIAL AREALRDLLS
     IQNRQISVEN IQKTVADYYK IKVADMYSKK RPASIARPRQ IAMYLAKELT QKSLPEIGEL
     FGGRDHTTVL HAVRKISGER QQLTELNQQL HVLEQTLKG
//
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