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Database: UniProt
Entry: A0A0J1DGV2_9BURK
LinkDB: A0A0J1DGV2_9BURK
Original site: A0A0J1DGV2_9BURK 
ID   A0A0J1DGV2_9BURK        Unreviewed;       474 AA.
AC   A0A0J1DGV2;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   25-OCT-2017, entry version 18.
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=AB595_00135 {ECO:0000313|EMBL:KLU38328.1};
OS   Massilia sp. WF1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Massilia.
OX   NCBI_TaxID=1406431 {ECO:0000313|EMBL:KLU38328.1, ECO:0000313|Proteomes:UP000036336};
RN   [1] {ECO:0000313|Proteomes:UP000036336}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|Proteomes:UP000036336};
RA   Lou J., Gu H., Wang H., Xu J.;
RT   "High quality genome sequence of a efficient PHE-degrading Massilia
RT   sp. strain WF1, isolated from a polycyclic aromatic hydrocarbons
RT   (PAHs) contaminated soil.";
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:KLU38328.1}.
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DR   EMBL; LELH02000001; KLU38328.1; -; Genomic_DNA.
DR   RefSeq; WP_047821174.1; NZ_LELH02000001.1.
DR   EnsemblBacteria; KLU38328; KLU38328; AB595_00135.
DR   PATRIC; fig|1406431.3.peg.24; -.
DR   Proteomes; UP000036336; 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:UP000036336};
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:UP000036336}.
FT   DOMAIN      171    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     179    186       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   474 AA;  53458 MW;  C45258270929A01C CRC64;
     MENFWQACST QLELELTPQQ YTAWIKPLVA LDYEDGKLRI AAPNRFKLDW VKSQFANRIT
     ALASDFWERP VEVQFVLDPR NLPKKPDAVS NRQPTSSTAE MAAGAIGINA AADNTVPATP
     VVTPDNVIAN NPRREQSRVN PELTFENFVT GKANQLARAA AIQVANNPGV SYNPLFFYGG
     VGLGKTHLIH AIGNQVMADQ PGARIRYIHA EQYVRDVVTA YQRKGFDDFK HYYHSLDMLL
     IDDIQFFGGK SRTQEEFFYA FEALIAAKKQ IIITSDTYPK EITGMDDRLI SRFDSGLTVA
     IEPPELEMRV AILMKKAESE GVVLNDDVAF FVAKHLRSNV RELEGALRKI LAYSRFHGKE
     ITIDVVKEAL KDLLSVQNRQ ISVENIQKTV ADFFNIKVAD MYSKRRPANI ARPRQIAMYL
     AKELTQKSLP EIGELFGGRD HTTVLHAVRK IAQDRQKNAE CNHELHVLEQ TLKG
//
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