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Database: UniProt
Entry: A0A0G1TJI0_9BACT
LinkDB: A0A0G1TJI0_9BACT
Original site: A0A0G1TJI0_9BACT 
ID   A0A0G1TJI0_9BACT        Unreviewed;       452 AA.
AC   A0A0G1TJI0;
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=UY07_C0006G0009 {ECO:0000313|EMBL:KKU81929.1};
OS   Parcubacteria group bacterium GW2011_GWA1_47_8.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618793 {ECO:0000313|EMBL:KKU81929.1, ECO:0000313|Proteomes:UP000034272};
RN   [1] {ECO:0000313|EMBL:KKU81929.1, ECO:0000313|Proteomes:UP000034272}
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:KKU81929.1}.
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DR   EMBL; LCOP01000006; KKU81929.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU81929; KKU81929; UY07_C0006G0009.
DR   PATRIC; fig|1618793.3.peg.173; -.
DR   Proteomes; UP000034272; 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:UP000034272};
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:UP000034272}.
FT   DOMAIN      150    284       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   452 AA;  52361 MW;  2448BC763F672A03 CRC64;
     MSDNTQLWEK TLSSIEGELS RANFSTWFKN TIIIKQDDGM VIVGVPNEFV KDWLQNKFHK
     TILRSLRNLS EHIRGVEYLV HKVEDSKTVR PQDGKVVFNQ QTELPLNDLY VNREDGLNPR
     YTFDNFIIGS FNELAYAASQ AILQKVGTNV YNPLFIYGKT GLGKTHLIQA IGNQIKKHHP
     GKKVFYITSE KFTIDYVNSV SQGSKAMSVF KEKYRKYDLF IMDDIQFLSN KEKTQEELFH
     IFNELYNNNK QIVFSSDQHP NYIPTLENRL KSRFSSGMIV DVQEPEYESR LAILRAKAEV
     NDFCPPVEII EYLASSVQGN IRELEGLLNG IICQSQLKNK HLTLAEIKPF IKNTAKPKKL
     LSVKEIVKVV CDFYNIQEDY VYEKTRRKEV LKPRQVAMFI LREDFNISYP TIGQKLGGRD
     HTTVMHSCDK IKTDMKNDLS LIQEVDQIRA MF
//
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