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Database: UniProt
Entry: G8QHT7_DECSP
LinkDB: G8QHT7_DECSP
Original site: G8QHT7_DECSP 
ID   G8QHT7_DECSP            Unreviewed;       473 AA.
AC   G8QHT7;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-SEP-2017, entry version 45.
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=Dsui_0831 {ECO:0000313|EMBL:AEV25238.1};
OS   Dechlorosoma suillum (strain ATCC BAA-33 / DSM 13638 / PS) (Azospira
OS   oryzae).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Azospira.
OX   NCBI_TaxID=640081 {ECO:0000313|EMBL:AEV25238.1, ECO:0000313|Proteomes:UP000005633};
RN   [1] {ECO:0000313|EMBL:AEV25238.1, ECO:0000313|Proteomes:UP000005633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-33 / DSM 13638 / PS
RC   {ECO:0000313|Proteomes:UP000005633};
RX   PubMed=22535943; DOI=10.1128/JB.00124-12;
RA   Byrne-Bailey K.G., Coates J.D.;
RT   "Complete genome sequence of the anaerobic perchlorate-reducing
RT   bacterium Azospira suillum strain PS.";
RL   J. Bacteriol. 194:2767-2768(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; CP003153; AEV25238.1; -; Genomic_DNA.
DR   RefSeq; WP_014235939.1; NC_016616.1.
DR   STRING; 640081.Dsui_0831; -.
DR   EnsemblBacteria; AEV25238; AEV25238; Dsui_0831.
DR   KEGG; dsu:Dsui_0831; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005633; Chromosome.
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:UP000005633};
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:UP000005633}.
FT   DOMAIN      170    301       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      381    450       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     178    185       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  52602 MW;  21F1451FFB53203E CRC64;
     MSGFWSICLS QFEQELPPQQ FNTWIKPLRL EGEDNLAEGL RLLAPNGFIL KWVKERYLSR
     IEELAHSHFS APVAISLGIG GGRTAVAVAR PTAPAAAPAE IPAAAPRTMA PAPAAAPAPA
     PAARRNNGPQ SSYEKTRLIP GFTFDNLVVG KANDLARAAA MQVAQNPGVS YNPLFIYGGV
     GLGKTHVIHA IGNAILQADP DKVVRYVHAE DYYSDVVRAY QQKSFDVFKR YYKSLDVLLV
     DDVQFFNGKN RTQEEFFFVF NALTEAKKQI IITCDTYPKD INGLDDRLVT RFDWGLTVQI
     EPPETEMRVA ILKKKAEAEG VALDDEVAFF IAKHLRSNVR ELEGALKKVL AYSLFHGREI
     ALDLAKDALK DVIGAFNRQI TVENIQKTVA EYYKIKVADL YSKKRTRAIA RPRQVAMWLA
     KDLTPHSYPM IGDAFGGRDH TTVLHAVRTI DTLRAKDNEL NHDLHVLLQV LKG
//
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