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Database: UniProt
Entry: DNAA_STRU0
LinkDB: DNAA_STRU0
Original site: DNAA_STRU0 
ID   DNAA_STRU0              Reviewed;         451 AA.
AC   B9DSN7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   25-OCT-2017, entry version 57.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=SUB0001;
OS   Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=218495;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-854 / 0140J;
RX   PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA   Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A.,
RA   Barron A., Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A.,
RA   Field T.R., Maskell D., Kehoe M., Dowson C.G., Chanter N.,
RA   Whatmore A.M., Bentley S.D., Parkhill J.;
RT   "Evidence for niche adaptation in the genome of the bovine pathogen
RT   Streptococcus uberis.";
RL   BMC Genomics 10:54-54(2009).
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:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00377}.
DR   EMBL; AM946015; CAR40315.1; -; Genomic_DNA.
DR   RefSeq; WP_012657571.1; NC_012004.1.
DR   ProteinModelPortal; B9DSN7; -.
DR   SMR; B9DSN7; -.
DR   STRING; 218495.SUB0001; -.
DR   EnsemblBacteria; CAR40315; CAR40315; SUB0001.
DR   GeneID; 24162937; -.
DR   KEGG; sub:SUB0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000449; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
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:SF2; PTHR30050:SF2; 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; Complete proteome; Cytoplasm; DNA replication;
KW   DNA-binding; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    451       Chromosomal replication initiator protein
FT                                DnaA.
FT                                /FTId=PRO_1000189815.
FT   NP_BIND     152    159       ATP. {ECO:0000255|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   451 AA;  51626 MW;  E3C7426EA04D11B7 CRC64;
     MTENETIFWN RILELAQSQL KQTTYEFFVL DARLVKVENQ VATIYLDPMK ELFWEQNLKD
     VILTAGFEVF NAHISVNYQF EDDLASEIEE STSNHIFSRQ TINSLPAITS DLNPKYSFDN
     FIQGDENRWA VAASLAVANT PGTTYNPLFI WGGPGLGKTH LLNAIGNAVL LDNPKARVKY
     ITAENFINEF VIHIRLDTMD ELKEKFRNLD LLLIDDIQSL AKKTLLGTQE EFFNTFNALH
     NNNKQIVLTS DRTPDHLNDL EQRLVTRFKW GLTVNITPPD FETRVAILTN KIQEYNFTFP
     QDTIEYLAGQ FDSNVRDLEG ALKDISLVAN FKEIDKITVD IAAEAIRARK QDTPKMTIIP
     IEEIQTQVGK FYGVTVKEIK ATKRTQNIVL ARQVAMFLAR EMTDNSLPKI GKEFGGRDHS
     TVLHAYNKIK NMIIEDESLR IEIETIKNKI K
//
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