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Database: UniProt
Entry: I3TGF2_TISMK
LinkDB: I3TGF2_TISMK
Original site: I3TGF2_TISMK 
ID   I3TGF2_TISMK            Unreviewed;       525 AA.
AC   I3TGF2;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   05-JUL-2017, entry version 38.
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:AFK51840.1};
GN   OrderedLocusNames=TMO_0001 {ECO:0000313|EMBL:AFK51840.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK51840.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK51840.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK51840.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(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, 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; CP003236; AFK51840.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFK51840; AFK51840; TMO_0001.
DR   KEGG; tmo:TMO_0001; -.
DR   PATRIC; fig|1110502.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005258; 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:UP000005258};
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:UP000005258}.
FT   DOMAIN      222    353       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      433    502       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     230    237       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   525 AA;  58440 MW;  FFEDB4C6C2A14EF3 CRC64;
     MKPDDPRQLR LPLPMTSVSD PADFAEYEAQ WARVRDSLRT EFGDAAFYSW LKPLALASVA
     DGRVTIQVPT RFMRDWVVSH YADRIRVLWS WENPAVRRVD IAVAGVKPAA AEAPAQPAPR
     PAEVVDLPPV PMAAPAPMTS RSAVAVAPAR AAAPRAATAA APAIVIADGD AEAEAGSRAA
     ERIDQWSAGL DPRFTFDNFV CGKPNELAHA AALRVAESET VQFNPLFLYG GVGLGKTHLM
     HAIAWHIRGR NPRRKVVYMS AEKFMYEFIR ALRYKDTMAF KEQFRSVDVL MIDDVQFISG
     KDSTQEEFFH TFNALVDQNR QIVVSGDRSP SDLDGMEERL RSRLGWGMVA DIHPTTYELR
     LGILQQKADQ LGAAVPVKVL EFLAHKIASN VRELEGALNR VVAHATLVGR AITLETTQEV
     LQDLLRANER RLTIEDIQKR VAEHFNIRTS DMHSARRSRA IARPRQVAMY LAKQLTQSSL
     PEIGRKFGGR DHTTVMHAVK KVEELAAQDA GFSDDIELLR RMLES
//
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