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Database: UniProt
Entry: H8K2K9_RICAG
LinkDB: H8K2K9_RICAG
Original site: H8K2K9_RICAG 
ID   H8K2K9_RICAG            Unreviewed;       463 AA.
AC   H8K2K9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   05-JUL-2017, entry version 41.
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:AFC70051.1};
GN   OrderedLocusNames=MCE_06105 {ECO:0000313|EMBL:AFC70051.1};
OS   Rickettsia amblyommatis (strain GAT-30V) (Rickettsia amblyommii).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=1105111 {ECO:0000313|EMBL:AFC70051.1, ECO:0000313|Proteomes:UP000008005};
RN   [1] {ECO:0000313|Proteomes:UP000008005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAT-30V {ECO:0000313|Proteomes:UP000008005};
RA   Johnson S.L., Munk A.C., Han S., Bruce D.C., Dasch G.A.;
RT   "Complete genome sequence of Candidatus Rickettsia amblyommii strain
RT   GAT-30V.";
RL   Submitted (FEB-2012) 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; CP003334; AFC70051.1; -; Genomic_DNA.
DR   RefSeq; WP_014392565.1; NC_017028.1.
DR   EnsemblBacteria; AFC70051; AFC70051; MCE_06105.
DR   KEGG; ram:MCE_06105; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000008005; 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:UP000008005};
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:UP000008005}.
FT   DOMAIN      160    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      371    440       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     168    175       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   463 AA;  52932 MW;  4E0226AF71A9C1BB CRC64;
     MSTNQIILTD QGDNYVNVWS HVAQDLYNHY GETLYNSWFS KVNFIESSLN TVILCAPTNF
     VRDWIKSKYS MVILQLFQHY NNTIKSIEII TKELPGTTKT VIELPTKTFA DIGSSELNSE
     NIFSTLDVRF TFDNFVVGAP NELAYAAARA VAESSGAVSE SNPLFLYGGV GLGKTHLMHA
     IGWYIKQNNP SRKVIYMSAE KFMYQFVKAL RNKEVISFKE KFRSVDVLMI DDIQFICGKD
     STQEEFFHTF NTLIDNNRQM VISCDRSPSD LDNIEDRIKS RLGWGLVADV HSTTYELRLG
     ILESKIEQMN VKIPKDVIDF LASKIVSNVR ELEGALNKVI AHSNFTLKEI TLENTQNILR
     DLLRSNERII TVEDIQKKVA SRYNIKLSDM SSSRRLREVA RPRQIAMYLS KALTPKSLAD
     IGKKFGKKDH TTVMHAIKKV EELLENDIEL REEINLLMKI LQN
//
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