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Database: UniProt
Entry: D2NQA7_ROTMD
LinkDB: D2NQA7_ROTMD
Original site: D2NQA7_ROTMD 
ID   D2NQA7_ROTMD            Unreviewed;       564 AA.
AC   D2NQA7;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   05-JUL-2017, entry version 58.
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   OrderedLocusNames=RMDY18_00010 {ECO:0000313|EMBL:BAI63833.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI63833.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
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:SAAS00731907}.
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; AP011540; BAI63833.1; -; Genomic_DNA.
DR   RefSeq; WP_012902629.1; NC_013715.1.
DR   STRING; 680646.RMDY18_00010; -.
DR   EnsemblBacteria; BAI63833; BAI63833; RMDY18_00010.
DR   GeneID; 25056595; -.
DR   KEGG; rmu:RMDY18_00010; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; AGKEHTQ; -.
DR   Proteomes; UP000001883; 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; 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   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:UP000001883};
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:UP000001883}.
FT   DOMAIN      252    386       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      466    535       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     260    267       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   564 AA;  62264 MW;  F875F7C6FFB54C3D CRC64;
     MTDSLQARWA HLLSILAADP AVTARQRGFV NLAQPQGLMG SSRLIIEVPN KLTRAVFEEQ
     ISASFRAALH EAFGPSTTAL FDVNESMIPV EPASQDVFHG EREVHVEQAP AVAPAVPAHP
     EAPAGSRAFE YYTEPHPGPD HYEVPADEQV TRPSLHALEA ERAGFPSAQQ AAPVAPVAGA
     PREYPAPTFV PDAPAVPEAQ QVHPHEDPEN APTWDSSARL NPNYTFDTFV IGQSNRFAHA
     SAFAVAEQPG IVYNPLFIYG GSGLGKTHLL HAIGHYTKYL YPNLRVRYVN SEEFTNDFIN
     SIRDDEGSSF KQIYRNVDVL LIDDIQFLAG KEATMEEFFH TFNALYNHQK QIVITSDLPP
     KQLTGFAERM RSRFGSGLNV DVQPPELETR IAILRKKAQN EILPVRDDVM EYIASHVTAN
     IRELEGALIR ASAAASMKKP PEPITLAEAE TYLKDLLSDT GGAEITSALV LATVAKYFDV
     SIEDMQSKSR TRTLTNARQV AMYLLRELTE MSLPRIGNDL GGRDHTTVMH AVRKVSAQMA
     ERQTIFNQVT ELTNLIRQEQ RAAG
//
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