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Database: UniProt
Entry: B9NUJ8_9RHOB
LinkDB: B9NUJ8_9RHOB
Original site: B9NUJ8_9RHOB 
ID   B9NUJ8_9RHOB            Unreviewed;       460 AA.
AC   B9NUJ8;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   23-MAY-2018, entry version 60.
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:EEE36438.1};
GN   ORFNames=RKLH11_271 {ECO:0000313|EMBL:EEE36438.1};
OS   Rhodobacteraceae bacterium KLH11.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae.
OX   NCBI_TaxID=467661 {ECO:0000313|EMBL:EEE36438.1, ECO:0000313|Proteomes:UP000005135};
RN   [1] {ECO:0000313|Proteomes:UP000005135}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KLH11 {ECO:0000313|Proteomes:UP000005135};
RX   PubMed=21742885; DOI=10.1128/JB.05556-11;
RA   Zan J., Fricke W.F., Fuqua C., Ravel J., Hill R.T.;
RT   "Genome Sequence of Ruegeria sp. Strain KLH11, an N-Acylhomoserine
RT   Lactone-Producing Bacterium Isolated from the Marine Sponge Mycale
RT   laxissima.";
RL   J. Bacteriol. 193:5011-5012(2011).
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:SAAS00747961}.
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; DS999531; EEE36438.1; -; Genomic_DNA.
DR   RefSeq; WP_008755619.1; NZ_DS999531.1.
DR   STRING; 467661.RKLH11_271; -.
DR   EnsemblBacteria; EEE36438; EEE36438; RKLH11_271.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005135; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:UP000005135};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005135}.
FT   DOMAIN      152    282       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      368    437       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     160    167       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   460 AA;  52144 MW;  3D0250B402BE4F38 CRC64;
     MTQEKWGQLR NKLMKAVGKN NFTTWIEPLK FQELQDGVAV FSVPTNFMGN YVSQNFADLI
     LYELNTSGES VQRLAFRTAA NSSARPTLTE ETKPLSTPDA RPSVAETHSD SLEALQAAPL
     DARFTFDSFV VGKPNELAHA AARRVSEGGP VTFNPLVLYG GVGLGKTHLM HAIAWELKTK
     SPELNVLYLS AEQFMYRFVQ ALRERRMMDF KHLFRSVDVL MVDDVQFIAG KDSTQEEFFH
     TFNALVDQNK QIIISADRAP GEIKDLEDRV KSRLQCGLVV DLHPTDYELR LGILQNKVQQ
     YSSTYPDLTI SDGVLEFLAQ RISTNVRVLE GALTRLFAFA SLVGREIDMD LTQDCLADVL
     RMSERKITVE EIQRKVSEYY NIRLSDIIGP KRLRSYARPR QVAMYLCKQL TSRSLPEIGR
     RFGGRDHTTV MHGVKRIEEL KLTDGQIAED VEMLRRALEA
//
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