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Database: UniProt
Entry: A0A0L0LMM1_9BACT
LinkDB: A0A0L0LMM1_9BACT
Original site: A0A0L0LMM1_9BACT 
ID   A0A0L0LMM1_9BACT        Unreviewed;       453 AA.
AC   A0A0L0LMM1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 14.
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:KND51210.1};
GN   ORFNames=ABA06_02780 {ECO:0000313|EMBL:KND51210.1};
OS   Parcubacteria bacterium C7867-001.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1659195 {ECO:0000313|EMBL:KND51210.1, ECO:0000313|Proteomes:UP000037027};
RN   [1] {ECO:0000313|EMBL:KND51210.1, ECO:0000313|Proteomes:UP000037027}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7867-001 {ECO:0000313|EMBL:KND51210.1};
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: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:KND51210.1}.
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DR   EMBL; LFCK01000002; KND51210.1; -; Genomic_DNA.
DR   EnsemblBacteria; KND51210; KND51210; ABA06_02780.
DR   PATRIC; fig|1659195.3.peg.539; -.
DR   Proteomes; UP000037027; 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:UP000037027};
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:UP000037027}.
FT   DOMAIN      152    283       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      362    431       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     160    167       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   453 AA;  52437 MW;  EF64EDB4D78682AC CRC64;
     MLESVMNKSD PRELWEYVLT QVELSISPAN FNTWFRESSI VKIEDGIVYV GVPSQFFRDW
     YQKKFHTLLL KIIRGVSFEY RNIEYLIVKD DRRKPKEVRR DRPNTELPLD EFYINKSDNL
     NPRYTFDTFV IGAFNELAHT AAQAAIKRPG ITYNPLFIYG ETGRGKTHLI QAIGNHFKKM
     YPNRKVFYLT SERFGNDYTD SIQAGTANRF KEKYRQYDLL IMDDVQFLTK REKTQEELFH
     LFNSLHDNNK QIIFSSDRPP QAIPDIADRL RGRFSSGMTV DIGEPDTESR IAIVRKKAAH
     HGIHLDDSVI EYIATSVSGS IRELEGVINS VVCHTQVKGI PPDLAEVRQS LRTFSRPTKT
     VSVKHVVSKV AEFYGIDEES IYEKTRRREV VRPRQVIMYL LREDFSVSYP TIGSKLGGRD
     HTTVIHSCEK VKREVIEDAE LAKEISDIRG LLV
//
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