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Database: UniProt
Entry: A0A0G1KBG8_9BACT
LinkDB: A0A0G1KBG8_9BACT
Original site: A0A0G1KBG8_9BACT 
ID   A0A0G1KBG8_9BACT        Unreviewed;       447 AA.
AC   A0A0G1KBG8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 26.
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=UW34_C0005G0010 {ECO:0000313|EMBL:KKT45124.1};
OS   Parcubacteria group bacterium GW2011_GWA2_44_15.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618831 {ECO:0000313|EMBL:KKT45124.1};
RN   [1] {ECO:0000313|EMBL:KKT45124.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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}.
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:KKT45124.1}.
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DR   EMBL; LCHY01000005; KKT45124.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT45124; KKT45124; UW34_C0005G0010.
DR   PATRIC; fig|1618831.3.peg.169; -.
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   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}.
FT   DOMAIN      147    279       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     155    162       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      426    446       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   447 AA;  50963 MW;  FC6F61AAD4D87AB3 CRC64;
     MDNQQLWNNV LVEIELAVSK ANFNTWFKDT WILKQEDGVV FVSVPNTFAK DWLFNKYHKT
     ILKSLRTLSA NIRALEYLVA KDDGKRKDGA LPRGPVGPAA ELPLSDFYID KENNLNPKYT
     FESFVVGPFN ELAHAAAQAV VKKPGTTYNP LFIYGNTGHG KTHLIQAVGN HIRRMDPSKK
     IFYVTSEKFS LDYVSSVQAN KTIQFKEKYR KYDILIMDDI QFLANKESTQ EELFHLFNSL
     HETNRQIVFS SDKHPNFIPN LEDRLKSRFS AGMIIDIPTP DRESRLAILQ TKVRNSGVYL
     APDVLDHLAT SVDGNIRELE GMLNVLICQS QLKGKDLGIT EVRNLIKNSA KPKKAVSVKE
     VTKAVSSFFN IEEGDIYEKT RRKEVVKPRQ LVMYILRQDF GVSYPLIGQK LGGRDHTTVI
     HSCEKIKEEL KLNSALEQEI NQIRAML
//
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