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Database: UniProt
Entry: I2F1F5_9BACT
LinkDB: I2F1F5_9BACT
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ID   I2F1F5_9BACT            Unreviewed;       447 AA.
AC   I2F1F5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   16-JAN-2019, entry version 51.
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   ORFNames=Theba_0001 {ECO:0000313|EMBL:AFK05758.1};
OS   Mesotoga prima MesG1.Ag.4.2.
OC   Bacteria; Thermotogae; Kosmotogales; Kosmotogaceae; Mesotoga.
OX   NCBI_TaxID=660470 {ECO:0000313|EMBL:AFK05758.1, ECO:0000313|Proteomes:UP000002881};
RN   [1] {ECO:0000313|EMBL:AFK05758.1, ECO:0000313|Proteomes:UP000002881}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MesG1.Ag.4.2 {ECO:0000313|EMBL:AFK05758.1};
RX   PubMed=22798451;
RA   Zhaxybayeva O., Swithers K.S., Foght J., Green A.G., Bruce D.,
RA   Detter C., Han S., Teshima H., Han J., Woyke T., Pitluck S., Nolan M.,
RA   Ivanova N., Pati A., Land M.L., Dlutek M., Doolittle W.F., Noll K.M.,
RA   Nesbo C.L.;
RT   "Genome Sequence of the Mesophilic Thermotogales Bacterium Mesotoga
RT   prima MesG1.Ag.4.2 Reveals the Largest Thermotogales Genome To Date.";
RL   Genome Biol. Evol. 4:700-708(2012).
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}.
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; CP003532; AFK05758.1; -; Genomic_DNA.
DR   RefSeq; WP_006487417.1; NC_017934.1.
DR   STRING; 660470.ThebaDRAFT_1744; -.
DR   EnsemblBacteria; AFK05758; AFK05758; Theba_0001.
DR   KEGG; mpg:Theba_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; MPRI660470:G1GN1-1-MONOMER; -.
DR   Proteomes; UP000002881; 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   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; 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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002881};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002881}.
FT   DOMAIN      135    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     143    150       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  50688 MW;  D6DBBDD3AB67BFE7 CRC64;
     MSNSIISTLK KKVSKKTWDN WFSTFELKAV EDERVVFSVA NLFIKDWLQT KYGAVISDSI
     AEILGRRVSF EIVYKNKETP SVDSTSDQIS GSLLKRKPLM ISNLNPEYTF SNFVVGSENK
     ALYEVALDVT QNPGKYNPFF VYGGVGLGKT HLLQAIAQET MSNFPDKKVL YITSEQFMND
     MIQSIKENNI QKFRDHYRKK SDILLIDDIQ FLIGKKGVQN EFFHSFNELH DSGKQLIICS
     DRNPEELETF HSRLKSRFQM GMLMSIQEPR PSTRFHIAKQ LAQRESVSLP DDVAKVLADN
     IDGNLRRLRG AIIKLIVHSS VFRSQIDLSL ATQILQSFTG SINVPAFQRP IDQIYSAIEK
     TMKVTKKEIE SGSRSKDIVL ARQLTMYILK NHFGKQVTEI ARETGKQHST VIHSLKKIDK
     SVMMGKGATK LLYDDVIGII TSNSAAV
//
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