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Database: UniProt
Entry: A0A0G1TL04_9BACT
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ID   A0A0G1TL04_9BACT        Unreviewed;       429 AA.
AC   A0A0G1TL04;
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=UY09_C0012G0016 {ECO:0000313|EMBL:KKU82512.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_8.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618847 {ECO:0000313|EMBL:KKU82512.1, ECO:0000313|Proteomes:UP000034914};
RN   [1] {ECO:0000313|EMBL:KKU82512.1, ECO:0000313|Proteomes:UP000034914}
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:KKU82512.1}.
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DR   EMBL; LCOR01000012; KKU82512.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU82512; KKU82512; UY09_C0012G0016.
DR   PATRIC; fig|1618847.3.peg.225; -.
DR   Proteomes; UP000034914; 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:UP000034914};
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:UP000034914}.
FT   DOMAIN      126    258       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      336    405       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     134    141       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   429 AA;  48990 MW;  60785D3FE319B92D CRC64;
     MNAQEIWDAS LAELELIISK AIFNTWFKCT RALEVKGTDL IIAVPSIFNR EWLDQKHAEV
     IIKTVRSIAP EVRSIKNLIX XXXXXXXXXX XSGINPRYRF ENFIVGPFNE LAHAAAQSVA
     NSPGTRYNPL FVYGGVGLGK THLLQSIGNR LLEHNKNAKV LYISSEKFTS DLVNAIRSQT
     TDAFQQFYRQ VDLLIIDDVQ FIAGKEKTQE EFFHTFNHLY QSGKQIVLSS DRPPKSIPTL
     EGRLRSRFEG GMPVDIGAPD YETRVAILRQ KCEEFDVLLD GTIIDLIATK ITQNIRELEG
     ALNRLVALNE LGGELSKEKI EEVVAEFSSN TQKSINPQKI IDAVALHFDI NKEDLLRKNR
     RKEIAMPRQL IMYLLRTKLQ QSFPEIGRRL GGRDHTTVMY AVDKIERKLK TSQEFKEKLD
     MITDRIYNY
//
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