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Database: UniProt
Entry: J9DZ63_9PROT
LinkDB: J9DZ63_9PROT
Original site: J9DZ63_9PROT 
ID   J9DZ63_9PROT            Unreviewed;       497 AA.
AC   J9DZ63;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   05-JUL-2017, entry version 33.
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=IMCC14465_07750 {ECO:0000313|EMBL:EJW20979.1};
OS   alpha proteobacterium IMCC14465.
OC   Bacteria; Proteobacteria; Alphaproteobacteria.
OX   NCBI_TaxID=1220535 {ECO:0000313|EMBL:EJW20979.1, ECO:0000313|Proteomes:UP000004836};
RN   [1] {ECO:0000313|EMBL:EJW20979.1, ECO:0000313|Proteomes:UP000004836}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC14465 {ECO:0000313|EMBL:EJW20979.1,
RC   ECO:0000313|Proteomes:UP000004836};
RX   PubMed=23209213; DOI=10.1128/JB.01888-12;
RA   Yang S.J., Kang I., Cho J.C.;
RT   "Genome Sequence of Strain IMCC14465, Isolated from the East Sea,
RT   Belonging to the PS1 Clade of Alphaproteobacteria.";
RL   J. Bacteriol. 194:6952-6953(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}.
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:EJW20979.1}.
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DR   EMBL; ALYF01000003; EJW20979.1; -; Genomic_DNA.
DR   EnsemblBacteria; EJW20979; EJW20979; IMCC14465_07750.
DR   PATRIC; fig|1220535.3.peg.772; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004836; Unassembled WGS sequence.
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:UP000004836};
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:UP000004836}.
FT   DOMAIN      189    317       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      405    474       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     197    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   497 AA;  56935 MW;  D50E4D04C8136B5E CRC64;
     MSEENTNENR QDKNANKNTN KNTDDLTIAK RQWDRVRSRL RAELGEATFN SWFRHLEILK
     ATSASVTIQV PTRFIGSWIE TNYLKRILGH WKKEDEAINK INITIQPAMH QPAAQPETIS
     RVVSDNRAPQ AVQNAAPPQA LTEERAQDDV GAPLEPRYTF DNFVVGKSNE MAHAAARRIT
     DGDPSYYKLH NPLFLYGGVG LGKTHLMHAI AWEIRRNDPS RRVIYTSAEK FMYQFIRALR
     YKDMMSFKQQ FREVDVLMVD DIQFIAGKES TQEEFFHTFN ALIDGNHQVI ISADRSPSDL
     EGIEERIRSR LGWGLVADIH PTDYELRLGI LQSKAETLVR NHKDASVPEQ VLEFLAQRVA
     TNIRELEGAL NRVVAFASFS GRPITLEMAK EILRDLLRAS ERRISIDQIQ RKVADYYNVR
     MGDMLSARRS RAVARPRQIA MYLSKQLTTR SLPEIGRKFG GRDHTTVIHA VRKVESLRES
     DPSIEEDVDL LLRSLEA
//
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