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Database: UniProt
Entry: A0A0F9YVH9_9BACT
LinkDB: A0A0F9YVH9_9BACT
Original site: A0A0F9YVH9_9BACT 
ID   A0A0F9YVH9_9BACT        Unreviewed;       499 AA.
AC   A0A0F9YVH9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-SEP-2017, entry version 16.
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=UR26_C0004G0016 {ECO:0000313|EMBL:KKP35469.1};
OS   candidate division TM6 bacterium GW2011_GWF2_32_72.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619079 {ECO:0000313|EMBL:KKP35469.1, ECO:0000313|Proteomes:UP000034766};
RN   [1] {ECO:0000313|EMBL:KKP35469.1, ECO:0000313|Proteomes:UP000034766}
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:KKP35469.1}.
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DR   EMBL; LBON01000004; KKP35469.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP35469; KKP35469; UR26_C0004G0016.
DR   PATRIC; fig|1619079.3.peg.663; -.
DR   Proteomes; UP000034766; 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: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:UP000034766};
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:UP000034766}.
FT   DOMAIN      193    324       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      406    475       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     201    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   499 AA;  56371 MW;  D63928C8CCDF91C8 CRC64;
     MLGTSVKLRK IIVPLTIFVE LLVIKGIWEE FLKIAKEEAG SRVVETWLKA ITFQEWDAIN
     KIASLKAPND FVRNWVEKNY MNLLTINLSR LFNVDKVSVI FESENKKEEL LGSALTCAKS
     VEVTPALTMI PATVIKPSKQ STKTKSAVVA NRNFDSYLFG LNKAHSFSAY VLGESNSLAY
     SAARAVAENP GKLYNPLLIY GGPGLGKTHL IHAIGNHVKE LFPKSNVLYQ TADRFVSEFI
     SAIRFDKMHQ FQAKYRTIDV LLIDDIQFIA NKEQSQEAFF HVFNYLYEAK KQVVLTCDVL
     PGEIKGLADR LRSRLEWGMV TDIQPPEQAM KIEILKRKVQ VSTEEHVEEA VLSFIASRFK
     GNVRELEGGL IRVLAFANLT KQPITMDLAQ KVLQKVPEKQ NGPCAGLDLI AKEVCKQYAV
     ELNDLKCQGR RKEVAFARQV AMFMMKQLTN KSLKEIGSFF GKKDHSTVLH ACSKIEEMQK
     LDPLFSHQYK TIKNHILNG
//
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