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Database: UniProt
Entry: A0A1Y0ETA0_9BURK
LinkDB: A0A1Y0ETA0_9BURK
Original site: A0A1Y0ETA0_9BURK 
ID   A0A1Y0ETA0_9BURK        Unreviewed;       493 AA.
AC   A0A1Y0ETA0;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   13-FEB-2019, entry version 14.
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   ORFNames=CCO03_00005 {ECO:0000313|EMBL:ARU06529.1};
OS   Comamonas serinivorans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=1082851 {ECO:0000313|EMBL:ARU06529.1, ECO:0000313|Proteomes:UP000196138};
RN   [1] {ECO:0000313|EMBL:ARU06529.1, ECO:0000313|Proteomes:UP000196138}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26136 {ECO:0000313|EMBL:ARU06529.1,
RC   ECO:0000313|Proteomes:UP000196138};
RA   Song R., Chenine A.L., Ruprecht R.M.;
RL   Submitted (MAY-2017) 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: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; CP021455; ARU06529.1; -; Genomic_DNA.
DR   KEGG; cser:CCO03_00005; -.
DR   KO; K02313; -.
DR   BioCyc; GCF_002158865:CCO03_RS00005-MONOMER; -.
DR   Proteomes; UP000196138; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000196138};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000196138}.
FT   DOMAIN      190    324       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      401    470       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     198    205       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      470    493       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   493 AA;  54506 MW;  6DC4D14BCFE631E4 CRC64;
     MTDTAEQASE GSEGAALWHA CLDVLAQDVP EQQFNTWIKP LVAQVSDDLS TVSLGVANRF
     KLDWVRAQYG TRIAEVLEAL AGQPVQVDLN ILARAPQPRI STTTARSVAR MGLQALSADA
     APEPETRPAS PAQATAEPAK PAKPNTAERE ASAFRSRLNP ALTFSTLVEG SANRMARAAA
     LHVASSPGQL YNPLFIYGGV GLGKTHLVHA VGNQLLADKL DAKVLYIHAE QFVSDVVKSY
     QRKTFDEFKA FYHSLDLLLI DDVQFFANKD RTQEEFFNAF EALLAKKSHI VMTSDTYPKG
     LTDIHERLVS RFDSGLTVAL EPPELELRVA ILINKAQTEG AVMPEDVAFF VAKNVRSNVR
     ELEGALRKIL AYSRFNQKEI SINLAREALR DLLSIQNRQI GVENIQKTVA DFYKIKVADM
     YSKKRPASIA RPRQIAMYLA KELTQKSLPE IGELFGGRDH TTVLHAVRKI AAERQTVTEL
     NQQLHVLEQT LKG
//
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