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Database: UniProt
Entry: A0A0G1G3H4_9BACT
LinkDB: A0A0G1G3H4_9BACT
Original site: A0A0G1G3H4_9BACT 
ID   A0A0G1G3H4_9BACT        Unreviewed;       469 AA.
AC   A0A0G1G3H4;
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   ECO:0000313|EMBL:KKT01812.1};
GN   ORFNames=UV80_C0008G0022 {ECO:0000313|EMBL:KKT01812.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_43_17.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619068 {ECO:0000313|EMBL:KKT01812.1, ECO:0000313|Proteomes:UP000034674};
RN   [1] {ECO:0000313|EMBL:KKT01812.1, ECO:0000313|Proteomes:UP000034674}
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:KKT01812.1}.
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DR   EMBL; LCFW01000008; KKT01812.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT01812; KKT01812; UV80_C0008G0022.
DR   PATRIC; fig|1619068.3.peg.953; -.
DR   Proteomes; UP000034674; 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:UP000034674};
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:UP000034674}.
FT   DOMAIN      154    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      377    446       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     162    169       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  53296 MW;  AD968778A5B2D1D5 CRC64;
     MKEFWIQVLA KMEPRVKRAH FVTWFQDTAV LSKKDGLLII GVPNVYARDW LENKLNGELI
     SAVREVDSAI LQISFEVHPN LGLADDKRGV DVKTLVDGGH SPRKVRGKQE VRLAEGVVSK
     CLNPKYTLQN FVVGQDNRLA HAACMAVSAS PGSSYNPLFV YGGVGLGKTH LLQATGNEIL
     RNYSDKVVVY MTSERFTNEI VEAIGKRSSK SFKDRYRNVD CLIIDDIQFL ANKEMTQVEF
     FHTFNELYDN GKQIIISSDK PPKELKGLEQ RLTSRFEMGM IVDVQFPDFE TRLAILHAKC
     REHQVLIAPE VLEFVAYNVR NSVRELEGVL LQAIAQSQLE QSTPTIRSVA RIVKKLNKID
     PLAGYDEKGD DRTVARSPDD VLSIVCKYYK IERDYLVGAD RHIGIMRPRQ IAMYLIKQEL
     RHSYEEIGRL FSGRNHTTVM HAVDKVLKTL RKDEGLLRDV NALKMEMGM
//
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