GenomeNet

Database: UniProt
Entry: A0A0G0VDR5_9BACT
LinkDB: A0A0G0VDR5_9BACT
Original site: A0A0G0VDR5_9BACT 
ID   A0A0G0VDR5_9BACT        Unreviewed;       479 AA.
AC   A0A0G0VDR5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=UU48_C0008G0010 {ECO:0000313|EMBL:KKR97801.1};
OS   Candidatus Uhrbacteria bacterium GW2011_GWF2_41_16.
OC   Bacteria; Candidatus Uhrbacteria.
OX   NCBI_TaxID=1618997 {ECO:0000313|EMBL:KKR97801.1, ECO:0000313|Proteomes:UP000034746};
RN   [1] {ECO:0000313|EMBL:KKR97801.1, ECO:0000313|Proteomes:UP000034746}
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}.
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:KKR97801.1}.
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; LCAU01000008; KKR97801.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKR97801; KKR97801; UU48_C0008G0010.
DR   PATRIC; fig|1618997.3.peg.759; -.
DR   Proteomes; UP000034746; 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; 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.
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:UP000034746};
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:UP000034746}.
FT   DOMAIN      174    305       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      386    455       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     182    189       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   479 AA;  55021 MW;  FA472CFE085F2AD6 CRC64;
     MRLLDPIPMN TNELWQAVLG ELELKLSKAN FTTWFKNTFI LVYENQELVI GVPNTFTKAW
     LEKKYHRDIT NLLQQFTSDR VRNVVYRVEI KTSPMNISIS DYSQEISDQT VSDVSFQQPV
     FSQTFTLPSL PRSYSETPEP SLNQKYAFSN FIVGKQNELA HAAAQAVSMQ PGGVYNPLFI
     YGGVGLGKTH LLQAVGNEIQ KRDPQAKILY ITCENFTNDF IHAVRTGRGK EFKDIYRNVD
     VLLIDDIQFI TGKEGTQEEF FHTFNALHQN NKQIILSSDR PPKAIPALEQ RLSSRFEWGM
     MTDIGSPDFE TRIAILEAKC REKKYLLDGE ILHHVATTIQ SNVRELEGAL NKIIAFHQFK
     NMIPTVESVK PILTSFQPTK MKKSVTTRQL IHTVALYYDL SIDDLLGKSR EKRLAFPRQI
     IMFLMREEMK CSYPSIGNEL GGRDHTTAMH AYDKITNQLT NDERLQHDIE TILQRLYVV
//
DBGET integrated database retrieval system