GenomeNet

Database: UniProt
Entry: A0A0G1NR96_9BACT
LinkDB: A0A0G1NR96_9BACT
Original site: A0A0G1NR96_9BACT 
ID   A0A0G1NR96_9BACT        Unreviewed;       458 AA.
AC   A0A0G1NR96;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 17.
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=UX33_C0003G0016 {ECO:0000313|EMBL:KKU22852.1};
OS   Candidatus Azambacteria bacterium GW2011_GWC1_46_13.
OC   Bacteria; Candidatus Azambacteria.
OX   NCBI_TaxID=1618619 {ECO:0000313|EMBL:KKU22852.1, ECO:0000313|Proteomes:UP000034569};
RN   [1] {ECO:0000313|EMBL:KKU22852.1, ECO:0000313|Proteomes:UP000034569}
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:SAAS00724167}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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:KKU22852.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LCLU01000003; KKU22852.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU22852; KKU22852; UX33_C0003G0016.
DR   PATRIC; fig|1618619.3.peg.87; -.
DR   Proteomes; UP000034569; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034569};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034569}.
FT   DOMAIN      149    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     157    164       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   458 AA;  52537 MW;  6557EF5517E09CB3 CRC64;
     MTKEELWQIV LSEIGIQISK ANFNTWLKNT SLTQNKDGEI VISVPNAFTK EWLENKYNKL
     ILKTLRNASN EIKEVKYVIC NNATAVLEET EKGAGRQKKA EEQMNFQELL INQETNLNPK
     YVFESFIVGS NNELANAAAL AITESIGTKY NPLFIYGGTG LGKTHLLQAL GNKVYKDHKG
     TKKIKYVTSE KFTNEVITSI RTKEMDNFKN KYRKIDVLII DDIQFLGGKE KTQEELFHIF
     NTLYERNKQI VFSSDRLPKE IPTIEDRLRS RFEGGMIADI GYPDLETRIA ILKSKTLEKG
     FFLADEVLTF IAANFQSNIR ELEGALNKIM AASNQMNVEK INVGMAEKIL SDIIGNSKKF
     TSVKQIFKSV SDFYDIQESG LIEKNRRKEI VKPRQIAMYL LREELKYSYP YIGSKLGGRD
     HTTVIHSCEK IEKELKTNQK MVEEINLIKK MIYKDANK
//
DBGET integrated database retrieval system