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Database: UniProt
Entry: A0A0G0N9K8_9BACT
LinkDB: A0A0G0N9K8_9BACT
Original site: A0A0G0N9K8_9BACT 
ID   A0A0G0N9K8_9BACT        Unreviewed;       385 AA.
AC   A0A0G0N9K8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 14.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
DE   Flags: Fragment;
GN   ORFNames=US96_C0052G0005 {ECO:0000313|EMBL:KKQ73796.1};
OS   Candidatus Woesebacteria bacterium GW2011_GWB1_38_5b.
OC   Bacteria; Candidatus Woesebacteria.
OX   NCBI_TaxID=1618569 {ECO:0000313|EMBL:KKQ73796.1, ECO:0000313|Proteomes:UP000034181};
RN   [1] {ECO:0000313|EMBL:KKQ73796.1, ECO:0000313|Proteomes:UP000034181}
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|RuleBase:RU000577}.
CC   -!- SIMILARITY: Belongs to the DnaA family.
CC       {ECO:0000256|RuleBase:RU004227, 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:KKQ73796.1}.
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DR   EMBL; LBUZ01000052; KKQ73796.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKQ73796; KKQ73796; US96_C0052G0005.
DR   Proteomes; UP000034181; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR001957; Chromosome_initiator_DnaA.
DR   InterPro; IPR020591; Chromosome_initiator_DnaA-like.
DR   InterPro; IPR013317; DnaA.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 1.
DR   Pfam; PF00308; Bac_DnaA; 1.
DR   Pfam; PF11638; DnaA_N; 1.
DR   PRINTS; PR00051; DNAA.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR00362; DnaA; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU000577};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034181};
KW   DNA replication {ECO:0000256|RuleBase:RU004227};
KW   DNA-binding {ECO:0000256|RuleBase:RU000577};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000577};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034181}.
FT   DOMAIN      146    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   NON_TER     385    385       {ECO:0000313|EMBL:KKQ73796.1}.
SQ   SEQUENCE   385 AA;  44249 MW;  66FD2A80D0F69B6A CRC64;
     METQELWNNV LLQIESSVSK ANFATWFKET KISGFDNGVV YLSVPNTFVQ EWLLKKFHQL
     ILKHLRESSE SIHALEYVIK EESETKNQYI PAKGAQGTRE LPLSEFYVNK DDNLNPRYTF
     ESFVVGPFNE LAYAAAQAVI KNPGVAYNPF FIYGSTGHGK THLIQAIGNA VKAADPSKKI
     YYFTSEKFIN DYIGSVQANK VSQFKERYRK YDMLIMDDVQ FLSGKEKTQE ELFHLFNIMK
     DSNKHIIFSC DKHPNFVTGL EDRLKSRFAA GMVTDIPAPD HESRVAIIKS KCSSINLFVE
     EDIIDYLADS IKGNIRDLEG VINLIVCQTE TKNKVLNLNE VKDLVKNSIK QKKLLSYKEV
     VKIISDFYKI EEESIYEKTR RKEVI
//
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