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Database: UniProt
Entry: A0A172TCK6_9DEIO
LinkDB: A0A172TCK6_9DEIO
Original site: A0A172TCK6_9DEIO 
ID   A0A172TCK6_9DEIO        Unreviewed;       456 AA.
AC   A0A172TCK6;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
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   ORFNames=SU48_00440 {ECO:0000313|EMBL:ANE44664.1};
OS   Deinococcus puniceus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE44664.1, ECO:0000313|Proteomes:UP000077363};
RN   [1] {ECO:0000313|EMBL:ANE44664.1, ECO:0000313|Proteomes:UP000077363}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY1 {ECO:0000313|EMBL:ANE44664.1,
RC   ECO:0000313|Proteomes:UP000077363};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL   Submitted (JAN-2015) 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; CP011387; ANE44664.1; -; Genomic_DNA.
DR   RefSeq; WP_064015748.1; NZ_CP011387.1.
DR   EnsemblBacteria; ANE44664; ANE44664; SU48_00440.
DR   KEGG; dpu:SU48_00440; -.
DR   PATRIC; fig|1182568.3.peg.91; -.
DR   KO; K02313; -.
DR   Proteomes; UP000077363; 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; 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:UP000077363};
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:UP000077363}.
FT   DOMAIN      146    274       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  51684 MW;  AE4ABC30447005EF CRC64;
     MSQEIWADVL GYVRKNISEV EYHTWFAPVK NLGVQEGSLV LGVRNSFAQE WFRKHYLELL
     EDALRSLGAQ NPAVSFQVLP AVQEAMFMPQ DAPPPPGPPP RSPSPAPFEN RKSLNPKYTF
     ENFVVGPNNN LAHAAALAVA ESPGKAYNPL FIYGDVGLGK THLMHAVGHY MMERFPGKRI
     EYVSTESFTN DLINAIRDDK MTLFRNRYRS VDLLLVDDIQ FLAGKERTQE EFFHTFNALY
     ENHKQIILSS DRPPRDIQTL EGRLRSRFEW GLITDIQSPE FETRVAILKM NAEHNRIDIP
     QDVLELIARQ VTSNIRELEG ALMRVVAFSS LNNVPFSRAV AAKALSNVFT PQEVKVEMID
     VLRQVAAHFN MPQDVVRGAG RVREVVVPRQ VAMYLIRELT SHSLPEIGQF FGRDHSTVMH
     AVSKVTEQMG KDTELTASVS SLRRRMQGLD EEENEA
//
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