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Database: UniProt
Entry: D5X2E3_THIK1
LinkDB: D5X2E3_THIK1
Original site: D5X2E3_THIK1 
ID   D5X2E3_THIK1            Unreviewed;       484 AA.
AC   D5X2E3;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   05-JUL-2017, entry version 51.
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   OrderedLocusNames=Tint_0001 {ECO:0000313|EMBL:ADG29417.1};
OS   Thiomonas intermedia (strain K12) (Thiobacillus intermedius).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Thiomonas.
OX   NCBI_TaxID=75379 {ECO:0000313|EMBL:ADG29417.1, ECO:0000313|Proteomes:UP000002185};
RN   [1] {ECO:0000313|EMBL:ADG29417.1, ECO:0000313|Proteomes:UP000002185}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 {ECO:0000313|EMBL:ADG29417.1,
RC   ECO:0000313|Proteomes:UP000002185};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ovchinnikova G., Kerfeld C.A., Cannon G.C.,
RA   Heinhorst S., Woyke T.;
RT   "Complete sequence of Thiomonas intermedia K12.";
RL   Submitted (APR-2010) 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; CP002021; ADG29417.1; -; Genomic_DNA.
DR   RefSeq; WP_013121833.1; NC_014153.1.
DR   EnsemblBacteria; ADG29417; ADG29417; Tint_0001.
DR   KEGG; tin:Tint_0001; -.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002185; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002185};
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:UP000002185}.
FT   DOMAIN      181    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      392    461       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     189    196       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      461    484       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   484 AA;  53843 MW;  556398B7F09A13A0 CRC64;
     MTQEQSWQQC CAQLATVIPD QQFAAWIKPL SSPHWSEDGN TAILHVPNRF KLDWLRSQYG
     ARITESLSAI VGRPVQVEFI VQKASARAAM HHSGALGLQS GSGSSSTSGS AQATHSADHA
     TPQQLAGPDG VSNAARDAAE ADALERSRLN PMLSFETLVT GKANQLARAA AIQVAENPGR
     SYNPLFIYGG VGLGKTHLMH AVGNALLAQQ PGARIRYLQA EQFVSEVVRA YQRKAFEEFK
     RYYHSLDLLL IDDVQFFAGK DKTQEEFFYA FEALITKRSQ IILTSDTYPK ELREMDQRLV
     SRFDSGLTVA IEPPELEMRV AILLRKADAE LAHLPEEVAF FVAKNVRSNV RELEGALRKI
     LAYARFSGQD VSIGLAKEAL KDLLSLQNRQ VSVENIQKTV ADFYKIKVAD MYSKKRPASI
     ARPRQIAMYL AKELTHKSLP EIGELFGGRD HTTVLHAVRK IGQERIKLQE LNQQLHVLEQ
     TLKA
//
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