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Database: UniProt
Entry: A0A0G0XSF8_9BACT
LinkDB: A0A0G0XSF8_9BACT
Original site: A0A0G0XSF8_9BACT 
ID   A0A0G0XSF8_9BACT        Unreviewed;       460 AA.
AC   A0A0G0XSF8;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   16-JAN-2019, entry version 27.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=UU84_C0006G0008 {ECO:0000313|EMBL:KKS27347.1};
OS   Candidatus Yanofskybacteria bacterium GW2011_GWC2_41_9.
OC   Bacteria; Candidatus Yanofskybacteria.
OX   NCBI_TaxID=1619029 {ECO:0000313|EMBL:KKS27347.1};
RN   [1] {ECO:0000313|EMBL:KKS27347.1}
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}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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:KKS27347.1}.
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DR   EMBL; LCCE01000006; KKS27347.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKS27347; KKS27347; UU84_C0006G0008.
DR   PATRIC; fig|1619029.3.peg.150; -.
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   Gene3D; 3.30.300.180; -; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
DR   InterPro; IPR024633; DnaA_N_dom.
DR   InterPro; IPR038454; DnaA_N_sf.
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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117}.
FT   DOMAIN      150    286       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED       85    105       {ECO:0000256|SAM:Coils}.
FT   COILED      324    344       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   460 AA;  53011 MW;  4283F7AA946A6E53 CRC64;
     MDLHELWKAA LGEIGLQISK ANYKTWLANT SIADKKNGVV IVAVPNSFTK EWLENKYHKF
     ILRSLRNIES EIKEVTYQIK PNYIKEELKD KKQTKEDELI IHKQLDFAEL NVDVETNLNP
     RYTFDNFIVG PSNELAHAAA SAIVKNLGNK YNPLFIYGGV GLGKTHLIQA IGNAVKKENC
     NKKIKYVTSE RFTSEVITTL RSGSLRPNDI DDFKKRWREI DLLIIDDIQF LSGKEKTQDE
     FFHTFNALYD AGKQIIISSD RPPKSIQTLE ERLRSRFEGG MIADISYPDL ETRITILKTK
     ANEKGFDFSY DIFEYIALNI KKNVRELEGA LNRLIASNLN ANKKDLNLTE VKKALNIIVN
     TPKKSTNFKN IIKAVAEFYD ISEKELLERS RKKEIVKPRQ IIMYLLREEL KSSFPFIGLK
     IGGRDHTTAI HACDKIKKEI ESDQNFNDEI NMIREKLYLV
//
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