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Database: UniProt
Entry: N9UQF5_9SPHN
LinkDB: N9UQF5_9SPHN
Original site: N9UQF5_9SPHN 
ID   N9UQF5_9SPHN            Unreviewed;       459 AA.
AC   N9UQF5;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   25-OCT-2017, entry version 34.
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:ENY80584.1};
GN   ORFNames=EBMC1_13713 {ECO:0000313|EMBL:ENY80584.1};
OS   Sphingopyxis sp. MC1.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=1174684 {ECO:0000313|EMBL:ENY80584.1, ECO:0000313|Proteomes:UP000013072};
RN   [1] {ECO:0000313|EMBL:ENY80584.1, ECO:0000313|Proteomes:UP000013072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC1 {ECO:0000313|EMBL:ENY80584.1,
RC   ECO:0000313|Proteomes:UP000013072};
RA   Lolas I.B., Kjeldal H., Almeida B., Le-Quy V., Gough H.L.,
RA   Nielsen J.L.;
RT   "Differential expression analysis of membrane associated proteins from
RT   triclosan-degrading sphingopyxis.";
RL   Submitted (FEB-2013) 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:SAAS00911680}.
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:ENY80584.1}.
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DR   EMBL; AOUN01000012; ENY80584.1; -; Genomic_DNA.
DR   EnsemblBacteria; ENY80584; ENY80584; EBMC1_13713.
DR   PATRIC; fig|1174684.3.peg.2770; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000013072; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000013072};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895}.
FT   DOMAIN      155    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      367    436       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  50642 MW;  50E14195C1276D7C CRC64;
     MEAMSADAAT LWPRVAEGLR RDLGARTFDH WLKPVRFAEY CTLSGVVTLE TASRFSANWI
     NERFGERLEL AWRQLLPAVR SVSVRGGVAA AERATVLASA PLPSFEASAP AAVPAANPAL
     LGFDPRLCFD RFVVARSNIL AANAARRMAM VETPQFNPLY LCSGTGQGKT HLLQAIAQDY
     AAAHPTATII LMSAEKFMLE FVGAMRGGDM MAFKARLRAA DLLLLDDLQF VIGKNSTQEE
     LLHTIDDLMT AGKRLVVTAD RPPAMLDGVE ARLLSRLSGG LVADIEAPED DLRERIIRQR
     LAAMPMVEVP DDVVAYLVRH FTRNIRELEG ALNKLLAYAA LTGARVDLAL AEDRLAENVR
     SARPRITIEE IQRAVCAHYR LDKAEMASKR RVRAVARPRQ VAMYLAKELT PRSYPEIGRR
     FGGRDHSTVI HAVRTVEALR VTDSELDAEI AAIRRSLNN
//
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