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Database: UniProt
Entry: A0A0G0C1C7_9BACT
LinkDB: A0A0G0C1C7_9BACT
Original site: A0A0G0C1C7_9BACT 
ID   A0A0G0C1C7_9BACT        Unreviewed;       478 AA.
AC   A0A0G0C1C7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-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   ECO:0000313|EMBL:KKP37062.1};
GN   ORFNames=UR28_C0034G0006 {ECO:0000313|EMBL:KKP37062.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_33_10.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619065 {ECO:0000313|EMBL:KKP37062.1, ECO:0000313|Proteomes:UP000034183};
RN   [1] {ECO:0000313|EMBL:KKP37062.1, ECO:0000313|Proteomes:UP000034183}
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:SAAS00911680}.
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:KKP37062.1}.
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DR   EMBL; LBOP01000034; KKP37062.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP37062; KKP37062; UR28_C0034G0006.
DR   PATRIC; fig|1619065.3.peg.1211; -.
DR   Proteomes; UP000034183; Unassembled WGS sequence.
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   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: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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034183};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034183}.
FT   DOMAIN      162    293       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      386    455       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     170    177       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   478 AA;  54540 MW;  28E8E22A33BBA7D0 CRC64;
     MTNLKDIWEP VLKIIEPKIG RRHFVTFFNN TALLGINNGV AKIGIISVFI RDWIDTKYRD
     MILDAIRSFD SSVIDLDFEI HSVLSSVEDL RSVKIVDNNA TTARSKSKTQ GRKIPNKEEV
     NVQGIRSKRL NSRYLLDNFV VGQGTRLAHA ACSAVASNPG SSYNPLFIYG GVGLGKTHLL
     HATGNEILKR HSNFAVVYTT AENFVNEIVE GIRTFKMNDI KKNYRKADCL IIDDVQFLAS
     RERTQEEFFH TFNELYDNHK QIILSSDRAP RELVGIEDRL RSRFEMGMMV DVGIPDYETR
     LAILQQKTMG HQAIIPLDVL EFIAYNIQDN VRALEGILLQ AIAKAKLEHT TPTVKMVARY
     IEKFDAKVEI QGDIHKYMPA NGSARTIDDV IEVVSAYYKI SHDEIKGSVR KREYLMPRQI
     SMYLCRVELN QSFEKIGLEF GGKNHTTVMN AYEKIKKLLD DDYNLVRDVN AIKREMGL
//
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