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Database: UniProt
Entry: I0HK09_RUBGI
LinkDB: I0HK09_RUBGI
Original site: I0HK09_RUBGI 
ID   I0HK09_RUBGI            Unreviewed;       481 AA.
AC   I0HK09;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   05-JUL-2017, entry version 43.
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:BAL93346.1};
GN   OrderedLocusNames=RGE_00010 {ECO:0000313|EMBL:BAL93346.1};
OS   Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Rubrivivax.
OX   NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL93346.1, ECO:0000313|Proteomes:UP000007883};
RN   [1] {ECO:0000313|EMBL:BAL93346.1, ECO:0000313|Proteomes:UP000007883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX   PubMed=22689232; DOI=10.1128/JB.00511-12;
RA   Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA   Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S.,
RA   Fujita N., Shimada K., Hanada S., Nagashima K.V.P.;
RT   "Complete genome sequence of phototrophic betaproteobacterium
RT   Rubrivivax gelatinosus IL144.";
RL   J. Bacteriol. 194:3541-3542(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}.
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DR   EMBL; AP012320; BAL93346.1; -; Genomic_DNA.
DR   RefSeq; WP_014426239.1; NC_017075.1.
DR   EnsemblBacteria; BAL93346; BAL93346; RGE_00010.
DR   KEGG; rge:RGE_00010; -.
DR   PATRIC; fig|983917.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; VENWVKD; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007883; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007883};
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:UP000007883}.
FT   DOMAIN      178    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      389    458       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     186    193       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      458    481       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   481 AA;  53034 MW;  BF05DB3875AC7F83 CRC64;
     MTVDLWQRGC ERLATELPEH QFNTWIRPLP PAQLSQDEAD AAVVSVRVPN RFKLDWIRAQ
     YAGRIESVLS DLAGKPVRLE LTLAPRAEAA APAPLRASNG YAHATVAAPA APAAAAALAA
     VASVTAAPSH PAPAASPAPA SNRHKLNPSL TFDTLVPGRA NQMARTAALH VAGAPGQMYN
     PLFIYGGVGL GKTHLVHAVG NALLKDRPDA RVLYLHAEQF ISDVVKNYQR KTFDELKAKY
     HSLDLLLIDD VQFFAGKDRT QEEFFNTFEA LLAKRAHIIM TSDTYPKGLV DIDERLTSRF
     DAGLTVAIEP PELEMRVAIL IKKALAEGAE MPEDVAFFIA KNVRANVREL EGALRKVLAY
     SRFSQKDINI ALTRDALKDL LSIQNRQISV ENIQKTVADF YKIKVADMYS KKRPASIARP
     RQIAMYLAKD MTKKSLPEIG ELFGGRDHTT VLHAVRKIAD ERQRNSELNQ QLHVLEQTLK
     G
//
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