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Database: UniProt
Entry: M9WVY8_9RICK
LinkDB: M9WVY8_9RICK
Original site: M9WVY8_9RICK 
ID   M9WVY8_9RICK            Unreviewed;       460 AA.
AC   M9WVY8;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   16-JAN-2019, entry version 44.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AGJ98462.1};
GN   ORFNames=wNo_00010 {ECO:0000313|EMBL:AGJ98462.1};
OS   Wolbachia endosymbiont of Drosophila simulans wNo.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Wolbachieae; Wolbachia.
OX   NCBI_TaxID=1236908 {ECO:0000313|EMBL:AGJ98462.1};
RN   [1] {ECO:0000313|EMBL:AGJ98462.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WNo {ECO:0000313|EMBL:AGJ98462.1};
RX   PubMed=23593012;
RA   Ellegaard K.M., Klasson L., Naslund K., Bourtzis K., Andersson S.G.;
RT   "Comparative genomics of wolbachia and the bacterial species
RT   concept.";
RL   PLoS Genet. 9:E1003381-E1003381(2013).
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:SAAS00756121}.
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}.
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DR   EMBL; CP003883; AGJ98462.1; -; Genomic_DNA.
DR   RefSeq; WP_015587641.1; NC_021084.1.
DR   EnsemblBacteria; AGJ98462; AGJ98462; wNo_00010.
DR   GeneID; 32546646; -.
DR   KEGG; wed:wNo_00010; -.
DR   PATRIC; fig|1236908.3.peg.1; -.
DR   KO; K02313; -.
DR   BioCyc; WEND1236908:WNO_RS00005-MONOMER; -.
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; IPR018312; Chromosome_initiator_DnaA_CS.
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.
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:SAAS00756129};
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      158    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   460 AA;  52900 MW;  18CBCAB82A602B3D CRC64;
     MNLINPKVST MFFDQIITVT DHNVTWEKIQ NYLHNLYGEA TYNSWLSSLR FISNRNGEVL
     LSVPTRFIKE WITVHYMEKI LSLWQSEDQS VCSIDIQLIE ERNSNSNTIL KNREENNHNL
     GSPLDTRFTF DNFVVGKSNE LAFTAAKRVA ESIDPISGSN PLFLYGGVGL GKTHLMHAIA
     WDIVNSPSAK RKVVYLSAEK FMYQYITALR SKDIMLFKEQ FRSVDVLMVD DVQFISGKDS
     TQEEFFHTFN ALIDQNKQLV ISADRSPSDL DGVEERIKSR LGWGLVADIN ETTFELRLGI
     LQAKVERMNM YVPKDVLEFL ARNIKSNIRE LEGALNKVAH TSLIGRSMTV ESASETLIDL
     LRSNHRSITI EEIQKKIAEF FNIKIADMQS NRRLRSLARP RQIAMYFAKK FTQKSLPDIG
     RNFGGRDHAT VIHAVKQVEN FIRTDPKFAD EINRLKKMFK
//
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