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Database: UniProt
Entry: D8P7E7_9BACT
LinkDB: D8P7E7_9BACT
Original site: D8P7E7_9BACT 
ID   D8P7E7_9BACT            Unreviewed;       446 AA.
AC   D8P7E7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   25-OCT-2017, entry version 49.
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:CBK39789.1};
GN   ORFNames=NIDE0001 {ECO:0000313|EMBL:CBK39789.1};
OS   Nitrospira defluvii.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
OX   NCBI_TaxID=330214 {ECO:0000313|EMBL:CBK39789.1, ECO:0000313|Proteomes:UP000001660};
RN   [1] {ECO:0000313|EMBL:CBK39789.1, ECO:0000313|Proteomes:UP000001660}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   DOI=10.1073/pnas.1003860107 ;
RA   Lucker S., Wagner M., Maixner F., Pelletier E., Koch H., Vacherie B.,
RA   Rattei T., Sinninghe Damste J., Spieck E., Le Paslier D., Daims H.;
RT   "A Nitrospira metagenome illuminates the physiology and evolution of
RT   globally important nitrite-oxidizing bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 0:0-0(2010).
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:SAAS00911680}.
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; FP929003; CBK39789.1; -; Genomic_DNA.
DR   RefSeq; WP_013246619.1; NC_014355.1.
DR   STRING; 330214.NIDE0001; -.
DR   EnsemblBacteria; CBK39789; CBK39789; NIDE0001.
DR   KEGG; nde:NIDE0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001660; Chromosome.
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: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.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001660};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001660}.
FT   DOMAIN      143    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      353    422       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     151    158       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   446 AA;  50578 MW;  C5FBF84E5633D79C CRC64;
     MWNDALVYIQ EKVPKQVFET WFTPVVLDRI EDTTAYLAVP NKFFGEWLGE HYRDLLAEAV
     SVAQGDGHLD VSFVVHNKQV PSTLPAQQES GSADTAGRGF VASRSKRGVQ LNPKYTFKSF
     VVGAGNQFAH AACMAVAEQP AKAYNPLFLY GGVGLGKTHL LNAIGNYLAE RSDLRIAYLT
     TEQFTNEVIN SIRYDKMIDL RKRYRNVDML MIDDIQFLAG KERTQEEFFH TFNTLYEAHK
     QIVLSSDRFP KDMPDIEERL RSRFEWGLIA DLQPPDVETR IAILRKKSED ERIALPEDVI
     HFLATTMKNN IRELEGSLVR VGAYSSLTGQ TITLDMAKNV LRDLIGDKKK IVSIEDIQEA
     VGSKYHLKIA DLKSRRRSKT LVHPRQIAMY LCRELTDASF PEIGRQFGGK DHTTIIHACR
     QISKAKEADS TLHTTLEGLK EQILRA
//
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