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Database: UniProt
Entry: A0A0C5J6B6_9RHOO
LinkDB: A0A0C5J6B6_9RHOO
Original site: A0A0C5J6B6_9RHOO 
ID   A0A0C5J6B6_9RHOO        Unreviewed;       459 AA.
AC   A0A0C5J6B6;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   25-OCT-2017, entry version 21.
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=PG1C_00010 {ECO:0000313|EMBL:AJP47253.1};
OS   Rugosibacter aromaticivorans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Rugosibacter.
OX   NCBI_TaxID=1565605 {ECO:0000313|EMBL:AJP47253.1, ECO:0000313|Proteomes:UP000061603};
RN   [1] {ECO:0000313|EMBL:AJP47253.1, ECO:0000313|Proteomes:UP000061603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG1-Ca6 {ECO:0000313|Proteomes:UP000061603};
RX   PubMed=25858839;
RA   Singleton D.R., Dickey A.N., Scholl E.H., Wright F.A., Aitken M.D.;
RT   "Complete Genome Sequence of a Novel Bacterium within the Family
RT   Rhodocyclaceae That Degrades Polycyclic Aromatic Hydrocarbons.";
RL   Genome Announc. 3:0-0(2015).
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}.
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DR   EMBL; CP010554; AJP47253.1; -; Genomic_DNA.
DR   EnsemblBacteria; AJP47253; AJP47253; PG1C_00010.
DR   KEGG; rbu:PG1C_00010; -.
DR   PATRIC; fig|1565605.3.peg.5; -.
DR   KO; K02313; -.
DR   Proteomes; UP000061603; Chromosome.
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:UP000061603};
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000061603}.
FT   DOMAIN      151    282       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     159    166       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   459 AA;  52666 MW;  B6B8E18D414C9EBB CRC64;
     MREFWSICLN WFEQELPAQQ FNTWIKGLRL EIDPNDNTQY QLIAPNRFIM QWVRERYLTQ
     IEKLGHEFFT HPITIQLSVN KSTPEIPTSH VEPESTTETL KKPLASPKNN DSDYTKTHLN
     HEFTFDTLVT GRANDLARAA AQQVAMNPGT SYNPLFIYGG VGLGKTHLIH AIGNSIYAAN
     PAMEIRYVHA EDYFSDMVRA FQQNSRDSFK QYYRSLDLLL IDDIQFFNRK DRTQEEFFYA
     FNALIEAKKQ IIITSDTYPK DVQGLEERLI SRFDWGLTVT IDPPELEMRI AILKKKAGAE
     NIPISDEVCF LIAKNLRSNV RELEGALNRV IAYAGFHGKE ISLDVAKDAL RDIISATNRQ
     ISLEQIQKTV SDFYKIKVSE LHSKKRTRAI ARPRQIAMWL ARELTSHSLP EIGDFFGGRD
     HTTVIHACRT ITEIKINDSE ISNNLHVLIQ TLKTSLVSG
//
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