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Database: UniProt
Entry: E3FHD3_STIAD
LinkDB: E3FHD3_STIAD
Original site: E3FHD3_STIAD 
ID   E3FHD3_STIAD            Unreviewed;       450 AA.
AC   E3FHD3;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   30-AUG-2017, entry version 50.
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:ADO67810.1};
GN   OrderedLocusNames=STAUR_0001 {ECO:0000313|EMBL:ADO67810.1};
OS   Stigmatella aurantiaca (strain DW4/3-1).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Archangiaceae; Stigmatella.
OX   NCBI_TaxID=378806 {ECO:0000313|EMBL:ADO67810.1, ECO:0000313|Proteomes:UP000001351};
RN   [1] {ECO:0000313|EMBL:ADO67810.1, ECO:0000313|Proteomes:UP000001351}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DW4/3-1 {ECO:0000313|EMBL:ADO67810.1,
RC   ECO:0000313|Proteomes:UP000001351};
RX   PubMed=21037205; DOI=10.1093/molbev/msq292;
RA   Huntley S., Hamann N., Wegener-Feldbrugge S., Treuner-Lange A.,
RA   Kube M., Reinhardt R., Klages S., Muller R., Ronning C.M.,
RA   Nierman W.C., Sogaard-Andersen L.;
RT   "Comparative genomic analysis of fruiting body formation in
RT   Myxococcales.";
RL   Mol. Biol. Evol. 28:1083-1097(2011).
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}.
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DR   EMBL; CP002271; ADO67810.1; -; Genomic_DNA.
DR   RefSeq; WP_013373925.1; NZ_AAMD01000004.1.
DR   STRING; 378806.STAUR_0001; -.
DR   EnsemblBacteria; ADO67810; ADO67810; STAUR_0001.
DR   KEGG; sur:STAUR_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001351; Chromosome.
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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001351};
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:UP000001351}.
FT   DOMAIN      147    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     155    162       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      426    450       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   450 AA;  50594 MW;  C985CD3DB7A4D62C CRC64;
     MSALAEALPA SPSAGMVWAR TLETIRQDGK TYALTWLERM CALDVREGAL VLGVPDRFFR
     DWVDDHYRAL LESTLARVGE GLGRVAYEVV EAPPPSVHLA PTPVTATNAM RPPRLSPRFT
     FGTFVVADSN QLPAAAAAAV ADKPGHHYNP LYIYGGTGLG KTHLLHAVGN LIWERNPAQR
     VVYLSSEQFT NEYVESVREH RMTEFRRKFR DECDVLLIDD IQFLGKREET QKEFFYTFNT
     LYEQNKAIVL TSDTVPSEIP GLEDRLRSRF AMGLLTDIRE PSYETRVAIL QKKAEAEGLG
     LPDDVAHFIA KHIQKNVREL EGALVKLSAI HSLSRLPVTV EFAAQVLKDI LPTHQSVDVE
     SIQREVARYY KVTVEALRED RRHKALAHAR QVAMYLSRKL TKSSFPEIAS RFNKDHSTVI
     SAVRKVEGLR ETDAGLKREL DELEAKLGGH
//
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