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Database: UniProt
Entry: A0A0G1FMJ7_9BACT
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ID   A0A0G1FMJ7_9BACT        Unreviewed;       486 AA.
AC   A0A0G1FMJ7;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=UW09_C0003G0142 {ECO:0000313|EMBL:KKT23620.1};
OS   candidate division TM6 bacterium GW2011_GWF2_43_87.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619086 {ECO:0000313|EMBL:KKT23620.1, ECO:0000313|Proteomes:UP000034056};
RN   [1] {ECO:0000313|EMBL:KKT23620.1, ECO:0000313|Proteomes:UP000034056}
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:KKT23620.1}.
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DR   EMBL; LCGZ01000003; KKT23620.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT23620; KKT23620; UW09_C0003G0142.
DR   PATRIC; fig|1619086.3.peg.684; -.
DR   Proteomes; UP000034056; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000034056};
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:UP000034056}.
FT   DOMAIN      180    308       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      391    460       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     188    195       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   486 AA;  55047 MW;  2371DDD8D07534F4 CRC64;
     MAVTIELIWQ DFLKIMHEEA GSRVVETWFK AVKFVRWDVL ERTVYLEAPN LFVKQWISSH
     YLELCQKHLS RLLSEEKVSV VFVDSTVSTP AIPPIPASSG PIVLMQLGEN AHKGGVELYQ
     AARPITSSEN RVKAVTARKK ADGFNGALME QYRFDTFVVG PSNALAFSAA QATVESRGKL
     YNPLFIYGGS GLGKTHLLHA IGNAVREQSR HRIVLYQSAD RFVHDFVLAI RQNKVHEFEA
     RYKDIDMLLV DDVQFISKKE QTQEAFFRIF NAMHQTGRQI IFTSDSMPCD IVGLAERVRS
     RLAGGLVADI QMPTLETKVA ILLKKAEANN YVLEDEIAYC IASCECSSVR ELEGMLIRVM
     AYASLTKQPL TEGVVRKVLT HTSEVKKEGA GLPSIARFVG KYFNYTVQEL RSSKRNKDLS
     QARHVAMYLM KRLTDASLRE IGIFFERKDH TTVLSALEKI EKHQRRDRLF ASELRKIEND
     LRSGNL
//
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