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Database: UniProt
Entry: G4E1U1_9GAMM
LinkDB: G4E1U1_9GAMM
Original site: G4E1U1_9GAMM 
ID   G4E1U1_9GAMM            Unreviewed;       456 AA.
AC   G4E1U1;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-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=ThisiDRAFT_0270 {ECO:0000313|EMBL:EGZ50585.1};
OS   Thiorhodospira sibirica ATCC 700588.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thiorhodospira.
OX   NCBI_TaxID=765914 {ECO:0000313|EMBL:EGZ50585.1, ECO:0000313|Proteomes:UP000003058};
RN   [1] {ECO:0000313|EMBL:EGZ50585.1, ECO:0000313|Proteomes:UP000003058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700588 {ECO:0000313|EMBL:EGZ50585.1,
RC   ECO:0000313|Proteomes:UP000003058};
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.,
RA   Frigaard N.-U., Bryant D., Woyke T.;
RT   "The draft genome of Thiorhodospira sibirica ATCC 700588.";
RL   Submitted (SEP-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:EGZ50585.1}.
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DR   EMBL; AGFD01000003; EGZ50585.1; -; Genomic_DNA.
DR   RefSeq; WP_006786271.1; NZ_AGFD01000003.1.
DR   EnsemblBacteria; EGZ50585; EGZ50585; ThisiDRAFT_0270.
DR   PATRIC; fig|765914.3.peg.280; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000003058; 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:UP000003058};
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:UP000003058}.
FT   DOMAIN      153    366       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      364    433       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     161    168       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  51625 MW;  5DB0289FC58DB7BE CRC64;
     MPGNSLWQQC IARLERELSD QQLNTWIRPL HAIDEEDTVR LLAPNRFVLD WVRKHFFARI
     ETLINECADG RTLRVQLEVG SQRAGAGKNG AERTTPLKKA NGKRHSITQL STPASQFTNN
     LNPNYTFDNF VEGKSNQLAR AASQQVADAH GKAYNPMFIY GGVGLGKTHL MHAIGNDILQ
     RNTTARVVYL HSERFVADMI KALQHNLMND FKRYYRSADA LLIDDIQFFA GKERSQEEFF
     HTFNALMEGH HQVIIACDRF PNEVNGLEER LKSRFGWGLT VAITPPELDT RIAILQNKAQ
     QAGLKLPNEV AYFMAKRIRA NIRELEGALR RILASAQFSG KPVDLAFAKE ALRDMLSAQE
     HLVSIENIQK IVSDYYKVSI ADMVSSKRTR AISRPRQMCM ALAKELTTNS LPQIGRSFGG
     RDHTTVLYAC RKVNELRKAD QEVDEAFNTL LQRLSG
//
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