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Database: UniProt
Entry: G2E1I9_9GAMM
LinkDB: G2E1I9_9GAMM
Original site: G2E1I9_9GAMM 
ID   G2E1I9_9GAMM            Unreviewed;       445 AA.
AC   G2E1I9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-SEP-2017, entry version 39.
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=ThidrDRAFT_2152 {ECO:0000313|EMBL:EGV31286.1};
OS   Thiorhodococcus drewsii AZ1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Chromatiaceae; Thiorhodococcus.
OX   NCBI_TaxID=765913 {ECO:0000313|EMBL:EGV31286.1, ECO:0000313|Proteomes:UP000004200};
RN   [1] {ECO:0000313|EMBL:EGV31286.1, ECO:0000313|Proteomes:UP000004200}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ1 {ECO:0000313|EMBL:EGV31286.1,
RC   ECO:0000313|Proteomes:UP000004200};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Vogl K., Liu Z., Imhoff J., Thiel V.,
RA   Frigaard N.-U., Bryant D.A., Woyke T.J.;
RT   "The draft genome of Thiorhodococcus drewsii AZ1.";
RL   Submitted (JUN-2011) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGV31286.1}.
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DR   EMBL; AFWT01000013; EGV31286.1; -; Genomic_DNA.
DR   EnsemblBacteria; EGV31286; EGV31286; ThidrDRAFT_2152.
DR   PATRIC; fig|765913.3.peg.2191; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004200; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-UniRule.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-UniRule.
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:UP000004200};
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:UP000004200}.
FT   DOMAIN      142    273       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      353    422       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   445 AA;  50001 MW;  D0A950069C4D1218 CRC64;
     MGLWDQCVKQ LKGELTSAEF NTWILPLQAR VDGGLLRLLA PNRFVLDWTQ KHYERRLIEL
     CAQFSDGSVC HIAFEVGGLD RERVTVAGHS RYEPPAPAPD MGERRASANL NADFTFDTFV
     EGKSNQLARA ASMQIGQNPG TAYNPLFIYG GVGLGKTHLM HAVGNVILAS NPSARVVYLH
     SERFVAEMIK ALQHNRIDEF KKTYRSVNAL LIDDVQFFAG KERSQEEFFH TFNALFESRQ
     QIVLSSDRFP KEVVGLEERL RSRFGWGLTV SIDPPDLETS VAILHCKATQ IGIELPEDVA
     FFVGRRIRSN IRELEGALRR LVANSQFTGK PITLEFAKHA LKDVLAAQDK QVSIENIQKT
     VAEYFKLRTS DLLSAKRSRS LARPRQIAMT LAKELTKHSL PEIGNAFGGR DHTTVLHATR
     KIKSLRDSDA GIEEDYKNLL RILTS
//
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