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Database: UniProt
Entry: D3ILI2_9BACT
LinkDB: D3ILI2_9BACT
Original site: D3ILI2_9BACT 
ID   D3ILI2_9BACT            Unreviewed;       469 AA.
AC   D3ILI2;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   05-JUL-2017, entry version 47.
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:EFC67655.1};
GN   ORFNames=HMPREF0670_02301 {ECO:0000313|EMBL:EFC67655.1};
OS   Prevotella sp. oral taxon 317 str. F0108.
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=575615 {ECO:0000313|EMBL:EFC67655.1, ECO:0000313|Proteomes:UP000003829};
RN   [1] {ECO:0000313|EMBL:EFC67655.1, ECO:0000313|Proteomes:UP000003829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0108 {ECO:0000313|EMBL:EFC67655.1,
RC   ECO:0000313|Proteomes:UP000003829};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ward D., Feldgarden M., Earl A., Young S.K., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E., Heiman D., Hepburn T., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Thomson T.,
RA   Walk T., White J., Yandava C., Izard J., Baranova O.V., Blanton J.M.,
RA   Tanner A.C., Dewhirst F.E., Haas B., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Prevotella sp. Oral Taxon 317 strain F0108.";
RL   Submitted (NOV-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: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; GG740075; EFC67655.1; -; Genomic_DNA.
DR   RefSeq; WP_009231395.1; NZ_GG740075.1.
DR   ProteinModelPortal; D3ILI2; -.
DR   STRING; 575615.HMPREF0670_02301; -.
DR   EnsemblBacteria; EFC67655; EFC67655; HMPREF0670_02301.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003829; Unassembled WGS sequence.
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   Complete proteome {ECO:0000313|Proteomes:UP000003829};
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:UP000003829}.
FT   DOMAIN      164    296       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      375    444       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   469 AA;  52935 MW;  C8F060205C35E0E6 CRC64;
     MDVTPDKHWE AALALIAQNV SPQQFDTWFK PIVFESFNNE TKLLVLRVPS SFVYEYIEEH
     YIDLLSRVLF SAFGQRIRLT YRVVVDSEHK KTQDIEADPA EAHATQAAKT WGAKQKAVEE
     PAKEQELDPQ LNPHQTFSNY IEGESNKLSR SVGLSVAEHP NTNQFNPMFI YGPSGCGKTH
     LVNAIGVQTK QLYPQKRVLY ISAHLFQVQF VNAVLKNATN DFIKFYQTID MLIVDDVQTW
     ASADKTQETF FHIFNHLFRN GKRIILASDR PPVELNEMSD RLITRFSCGI IAELEKPNVQ
     LCVDILNAKI RRDGLKIPAE VTQFIAETAN GSVRDLEGVI NSLMAYSVVY NSDIDMRLAE
     RVIKRAVKVD DTPLTVDDIL EKVSNHFNVS VSAVSSKSRK RDLVVPRQVS MYLAQKYTKM
     PASRIGKLVG GRDHSTVLHS CAQVEARLKT DSLFAAEVES IATSFKLKG
//
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