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Database: UniProt
Entry: A0A0J9E8K5_9RHOB
LinkDB: A0A0J9E8K5_9RHOB
Original site: A0A0J9E8K5_9RHOB 
ID   A0A0J9E8K5_9RHOB        Unreviewed;       450 AA.
AC   A0A0J9E8K5;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-SEP-2017, entry version 17.
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=AIOL_003997 {ECO:0000313|EMBL:KMW59016.1};
OS   Candidatus Rhodobacter lobularis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1675527 {ECO:0000313|EMBL:KMW59016.1, ECO:0000313|Proteomes:UP000037178};
RN   [1] {ECO:0000313|EMBL:KMW59016.1, ECO:0000313|Proteomes:UP000037178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IGS {ECO:0000313|EMBL:KMW59016.1};
RA   Jourda C., Santini S., Claverie J.-M.;
RT   "Draft genome sequence of an Alphaproteobacteria species associated to
RT   the Mediterranean sponge Oscarella lobularis.";
RL   Submitted (JUN-2015) 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:KMW59016.1}.
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DR   EMBL; LFTY01000002; KMW59016.1; -; Genomic_DNA.
DR   RefSeq; WP_049644560.1; NZ_LFTY01000002.1.
DR   EnsemblBacteria; KMW59016; KMW59016; AIOL_003997.
DR   PATRIC; fig|1675527.3.peg.4190; -.
DR   Proteomes; UP000037178; 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:UP000037178};
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:UP000037178}.
FT   DOMAIN      142    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   450 AA;  50260 MW;  045976DA61B972A5 CRC64;
     MDNATWGHIK ESLAGAVGKS NFSNWIEPLE FAQLQDGVAT FHVPTNFMGD WVQRNYADNI
     LGALTKSGAD VSRLKFAVSS GAPRQPAAKP TATPPAQAGH DAFGVPGAPL DPRFTFERFV
     VGKPNELAHA AAKRVAEGGE VTFNPLFLYG GVGLGKTHLM HAIAHELVTQ RPDLRVVYLS
     AEQFMYRFIQ ALREKQMMDF KQLFRSVDVL MVDDVQFIAG KDSTQEEFFH TFNALVDQHK
     QIIISADRAP GEIKDLEARI KSRLQSGLVV DLHPTDYELR LGILQQKTEQ QRAAHGNVPM
     ADGVLEFLAH RISTNVRVLE GALMRLFAFA SLVGKEISLE LTQDCLADIL READRKVTIE
     EIQRKVGEHY NVRLSDLIGP RRVRTIARPR QVAMWLAKKM TSRSLPEIGR RFGGRDHTTV
     MHGVRKIDEL RGTDSQIAED LELLRRALEA
//
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