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Database: UniProt
Entry: DNAA_ECOLI
LinkDB: DNAA_ECOLI
Original site: DNAA_ECOLI 
ID   DNAA_ECOLI              Reviewed;         467 AA.
AC   P03004; P78122; Q2M814;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 2.
DT   05-JUL-2017, entry version 166.
DE   RecName: Full=Chromosomal replication initiator protein DnaA;
GN   Name=dnaA; OrderedLocusNames=b3702, JW3679;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=K12;
RX   PubMed=6296774; DOI=10.1093/nar/10.22.7373;
RA   Hansen E.B., Hansen F.G., von Meyenburg K.;
RT   "The nucleotide sequence of the dnaA gene and the first part of the
RT   dnaN gene of Escherichia coli K-12.";
RL   Nucleic Acids Res. 10:7373-7385(1982).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6234204; DOI=10.1016/0378-1119(84)90253-1;
RA   Ohmori H., Kimura M., Nagata T., Sakakibara Y.;
RT   "Structural analysis of the dnaA and dnaN genes of Escherichia coli.";
RL   Gene 28:159-170(1984).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA   Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT   "DNA sequence and analysis of 136 kilobases of the Escherichia coli
RT   genome: organizational symmetry around the origin of replication.";
RL   Genomics 16:551-561(1993).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP   TO 403-407.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-22.
RX   PubMed=6329723;
RA   Hansen F.G., Hansen E.B., Atlung T.;
RT   "The nucleotide sequence of the dnaA gene promoter and of the adjacent
RT   rpmH gene, coding for the ribosomal protein L34, of Escherichia
RT   coli.";
RL   EMBO J. 1:1043-1048(1982).
RN   [7]
RP   REVIEW.
RX   PubMed=2558436; DOI=10.1016/0168-9525(89)90118-2;
RA   Georgopoulos C.;
RT   "The E. coli dnaA initiation protein: a protein for all seasons.";
RL   Trends Genet. 5:319-321(1989).
RN   [8]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA   Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
RN   [9]
RP   FUNCTION IN PLASMID DNA REPLICATION, AND DNA-BINDING.
RX   PubMed=9242693; DOI=10.1074/jbc.272.32.20173;
RA   Konieczny I., Doran K.S., Helinski D.R., Blasina A.;
RT   "Role of TrfA and DnaA proteins in origin opening during initiation of
RT   DNA replication of the broad host range plasmid RK2.";
RL   J. Biol. Chem. 272:20173-20178(1997).
RN   [10]
RP   FUNCTION IN AUTO REGULATION OF TRANSCRIPTION.
RC   STRAIN=K12;
RX   PubMed=16077105; DOI=10.1128/JB.187.16.5605-5613.2005;
RA   Riber L., Lobner-Olesen A.;
RT   "Coordinated replication and sequestration of oriC and dnaA are
RT   required for maintaining controlled once-per-cell-cycle initiation in
RT   Escherichia coli.";
RL   J. Bacteriol. 187:5605-5613(2005).
RN   [11]
RP   INTERACTION WITH DIAA, AND FUNCTION.
RX   PubMed=17699754; DOI=10.1101/gad.1561207;
RA   Keyamura K., Fujikawa N., Ishida T., Ozaki S., Su'etsugu M.,
RA   Fujimitsu K., Kagawa W., Yokoyama S., Kurumizaka H., Katayama T.;
RT   "The interaction of DiaA and DnaA regulates the replication cycle in
RT   E. coli by directly promoting ATP DnaA-specific initiation
RT   complexes.";
RL   Genes Dev. 21:2083-2099(2007).
RN   [12]
RP   IDENTIFICATION IN RIDA COMPLEX.
RX   PubMed=18977760; DOI=10.1074/jbc.M803158200;
RA   Su'etsugu M., Nakamura K., Keyamura K., Kudo Y., Katayama T.;
RT   "Hda monomerization by ADP binding promotes replicase clamp-mediated
RT   DnaA-ATP hydrolysis.";
RL   J. Biol. Chem. 283:36118-36131(2008).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 374-467.
RX   PubMed=12682358; DOI=10.1093/nar/gkg309;
RA   Fujikawa N., Kurumizaka H., Nureki O., Terada T., Shirouzu M.,
RA   Katayama T., Yokoyama S.;
RT   "Structural basis of replication origin recognition by the DnaA
RT   protein.";
RL   Nucleic Acids Res. 31:2077-2086(2003).
RN   [14]
RP   STRUCTURE BY NMR OF 2-108.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Structure and function of dnaA N-terminal domains: specific sites and
RT   mechanisms in inter-DNAA interaction and in dnaB helicase loading on
RT   oric.";
RL   Submitted (MAY-2007) to the PDB data bank.
CC   -!- FUNCTION: Plays a key role in the initiation and regulation of
CC       chromosomal replication. Binds in an ATP-dependent fashion to the
CC       origin of replication (oriC) to initiate formation of the DNA
CC       replication initiation complex exactly once per cell cycle. Binds
CC       the DnaA box (consensus sequence 5'-TTATC[CA]A[CA]A-3');
CC       subsequent binding of DNA polymerase III subunits leads to
CC       replisome formation. The DnaA-ATP form converts to DnaA-ADP; once
CC       converted to ADP the protein cannot initiate replication, ensuring
CC       only 1 round of replication per cell cycle. DnaA can inhibit its
CC       own gene expression as well as that of other genes such as dam,
CC       rpoH, ftsA and mioC.
CC   -!- FUNCTION: Also required for replication of plasmid DNA; binds 4
CC       dnaA boxes in the minimal plasmid RK2 replication origin (oriV).
CC   -!- SUBUNIT: Some 20 DnaA protein molecules bind their sites in oriC.
CC       Forms the RIDA (regulatory inactivation of DnaA) complex with ATP-
CC       DnaA, ADP-Hda and the DNA-loaded sliding beta clamp (dnaN).
CC       Interacts with DiaA; this stimulates the association of DnaA with
CC       the origin of replication. {ECO:0000269|PubMed:17699754,
CC       ECO:0000269|PubMed:18977760}.
CC   -!- INTERACTION:
CC       P66817:diaA; NbExp=5; IntAct=EBI-548951, EBI-1125806;
CC       P0ACB0:dnaB; NbExp=4; IntAct=EBI-548951, EBI-548978;
CC       P0ABT2:dps; NbExp=2; IntAct=EBI-548951, EBI-549640;
CC       P69931:hda; NbExp=2; IntAct=EBI-548951, EBI-545453;
CC       P0ACF0:hupA; NbExp=5; IntAct=EBI-548951, EBI-547648;
CC       P60422:rplB; NbExp=4; IntAct=EBI-548951, EBI-543515;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- MISCELLANEOUS: At least 4 systems specifically target DnaA to
CC       prevent more than 1 round of replication initiation per cell
CC       cycle. 1: SeqA binds to and sequesters hemimethylated oriC,
CC       preventing DnaA binding. 2: ATP-DnaA binds to the chromosomal datA
CC       locus, sequestering ATP-DnaA. 3: ATP-DnaA binds to its own
CC       promoter, repressing transcription. 4: RIDA (regulatory
CC       inactivation of DnaA) via Hda and the DNA-loaded beta clamp
CC       hydrolyzes ATP-DnaA to ADP-DnaA.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA62053.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; J01602; AAB59149.1; -; Genomic_DNA.
DR   EMBL; X01861; CAA25980.1; -; Genomic_DNA.
DR   EMBL; L10328; AAA62053.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC76725.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE77592.1; -; Genomic_DNA.
DR   PIR; G65172; IQECDA.
DR   RefSeq; NP_418157.1; NC_000913.3.
DR   RefSeq; WP_000059111.1; NZ_LN832404.1.
DR   PDB; 1J1V; X-ray; 2.10 A; A=374-467.
DR   PDB; 2E0G; NMR; -; A=2-108.
DR   PDBsum; 1J1V; -.
DR   PDBsum; 2E0G; -.
DR   ProteinModelPortal; P03004; -.
DR   SMR; P03004; -.
DR   BioGrid; 4261539; 146.
DR   DIP; DIP-9455N; -.
DR   IntAct; P03004; 44.
DR   MINT; MINT-207293; -.
DR   STRING; 316407.85676342; -.
DR   PaxDb; P03004; -.
DR   PRIDE; P03004; -.
DR   EnsemblBacteria; AAC76725; AAC76725; b3702.
DR   EnsemblBacteria; BAE77592; BAE77592; BAE77592.
DR   GeneID; 948217; -.
DR   KEGG; ecj:JW3679; -.
DR   KEGG; eco:b3702; -.
DR   PATRIC; fig|511145.12.peg.3826; -.
DR   EchoBASE; EB0231; -.
DR   EcoGene; EG10235; dnaA.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   InParanoid; P03004; -.
DR   KO; K02313; -.
DR   PhylomeDB; P03004; -.
DR   BioCyc; EcoCyc:PD03831; -.
DR   EvolutionaryTrace; P03004; -.
DR   PRO; PR:P03004; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IDA:EcoCyc.
DR   GO; GO:0003688; F:DNA replication origin binding; IMP:EcoCyc.
DR   GO; GO:0043565; F:sequence-specific DNA binding; IDA:EcoliWiki.
DR   GO; GO:0006260; P:DNA replication; IMP:EcoliWiki.
DR   GO; GO:0006270; P:DNA replication initiation; IBA:GO_Central.
DR   GO; GO:0008156; P:negative regulation of DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006275; P:regulation of DNA replication; IMP:EcoliWiki.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
DR   GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
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   1: Evidence at protein level;
KW   3D-structure; ATP-binding; Complete proteome; Cytoplasm;
KW   DNA replication; DNA replication inhibitor; DNA-binding;
KW   Nucleotide-binding; Reference proteome; Repressor; Transcription;
KW   Transcription regulation.
FT   CHAIN         1    467       Chromosomal replication initiator protein
FT                                DnaA.
FT                                /FTId=PRO_0000114174.
FT   NP_BIND     172    179       ATP. {ECO:0000305}.
FT   CONFLICT     69     70       AD -> RI (in Ref. 1). {ECO:0000305}.
FT   CONFLICT    403    407       VARPR -> GXGPG (in Ref. 3; AAA62053).
FT                                {ECO:0000305}.
FT   HELIX         5     16       {ECO:0000244|PDB:2E0G}.
FT   HELIX        21     24       {ECO:0000244|PDB:2E0G}.
FT   TURN         25     28       {ECO:0000244|PDB:2E0G}.
FT   STRAND       29     33       {ECO:0000244|PDB:2E0G}.
FT   STRAND       35     44       {ECO:0000244|PDB:2E0G}.
FT   HELIX        45     53       {ECO:0000244|PDB:2E0G}.
FT   HELIX        55     66       {ECO:0000244|PDB:2E0G}.
FT   STRAND       68     70       {ECO:0000244|PDB:2E0G}.
FT   STRAND       77     80       {ECO:0000244|PDB:2E0G}.
FT   HELIX       376    386       {ECO:0000244|PDB:1J1V}.
FT   HELIX       391    395       {ECO:0000244|PDB:1J1V}.
FT   HELIX       401    417       {ECO:0000244|PDB:1J1V}.
FT   HELIX       422    428       {ECO:0000244|PDB:1J1V}.
FT   HELIX       434    450       {ECO:0000244|PDB:1J1V}.
FT   HELIX       452    465       {ECO:0000244|PDB:1J1V}.
SQ   SEQUENCE   467 AA;  52551 MW;  607C8366A8CDCCED CRC64;
     MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW VRDKYLNNIN
     GLLTSFCGAD APQLRFEVGT KPVTQTPQAA VTSNVAAPAQ VAQTQPQRAA PSTRSGWDNV
     PAPAEPTYRS NVNVKHTFDN FVEGKSNQLA RAAARQVADN PGGAYNPLFL YGGTGLGKTH
     LLHAVGNGIM ARKPNAKVVY MHSERFVQDM VKALQNNAIE EFKRYYRSVD ALLIDDIQFF
     ANKERSQEEF FHTFNALLEG NQQIILTSDR YPKEINGVED RLKSRFGWGL TVAIEPPELE
     TRVAILMKKA DENDIRLPGE VAFFIAKRLR SNVRELEGAL NRVIANANFT GRAITIDFVR
     EALRDLLALQ EKLVTIDNIQ KTVAEYYKIK VADLLSKRRS RSVARPRQMA MALAKELTNH
     SLPEIGDAFG GRDHTTVLHA CRKIEQLREE SHDIKEDFSN LIRTLSS
//
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