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Database: UniProt
Entry: A0A0L0LNJ5_9BACT
LinkDB: A0A0L0LNJ5_9BACT
Original site: A0A0L0LNJ5_9BACT 
ID   A0A0L0LNJ5_9BACT        Unreviewed;       449 AA.
AC   A0A0L0LNJ5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   20-JUN-2018, entry version 20.
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:KND51530.1};
GN   ORFNames=AB202_03095 {ECO:0000313|EMBL:KND51530.1};
OS   Parcubacteria bacterium C7867-007.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659201 {ECO:0000313|EMBL:KND51530.1, ECO:0000313|Proteomes:UP000037534};
RN   [1] {ECO:0000313|EMBL:KND51530.1, ECO:0000313|Proteomes:UP000037534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-007 {ECO:0000313|EMBL:KND51530.1};
RX   PubMed=26257709; DOI=10.3389/fmicb.2015.00713;
RA   Nelson W.C., Stegen J.C.;
RT   "The reduced genomes of Parcubacteria (OD1) contain signatures of a
RT   symbiotic lifestyle.";
RL   Front. Microbiol. 6:713-713(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:SAAS00747961}.
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:KND51530.1}.
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DR   EMBL; LFCQ01000002; KND51530.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND51530; KND51530; AB202_03095.
DR   PATRIC; fig|1659201.3.peg.590; -.
DR   Proteomes; UP000037534; 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:UP000037534};
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:RU004227, 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:UP000037534}.
FT   DOMAIN      148    279       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      358    427       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  51933 MW;  838E0FD23AE911CC CRC64;
     MNRSDPHELW EYMLTQVELS ISSANFNTWF KESTIVKIED GIVYIGVPSQ FFRDWYQKKF
     HTLLLKIVRD VSYEFRNIEY MIVKDIARKP KEQRTRREPT PELPLNEFYI NKSDNLNPRY
     TFDTFVVGSF NELAHTAAMA AIARPGITYN PLFIYGDTGR GKTHLIQSIG NQYKKQYPNR
     KVFYLTSEKF GTDYTDSLQQ GTANRFKEKY RQYDLLIMDD VQFLSRKEKM QEELFHLFNT
     LYDNNKQIVF SSDRAPIAIP DIADRLRGRF VSGMTVDIGE PDSESRIAIV RKKAAMSGIT
     LSDEVAEYIA TSVTGSIREL EGVLNSVVCH TQVKGTPPDI AEVRQSLRSF SRPSKTVSVK
     HVVSKIAEFY GIEEESIYEK TRRREVVRPR QVIMYILRED FSVSYPTIGS KLGGRDHTTV
     IHSCEKVKRE VAEDTELAKE IQDIRTLLV
//
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