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Database: UniProt
Entry: A0A077J7B0_9BACI
LinkDB: A0A077J7B0_9BACI
Original site: A0A077J7B0_9BACI 
ID   A0A077J7B0_9BACI        Unreviewed;       448 AA.
AC   A0A077J7B0;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   25-OCT-2017, entry version 27.
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=HW35_09970 {ECO:0000313|EMBL:AIM16560.1};
OS   Bacillus sp. X1(2014).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1565991 {ECO:0000313|EMBL:AIM16560.1, ECO:0000313|Proteomes:UP000031100};
RN   [1] {ECO:0000313|Proteomes:UP000031100}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=X1 {ECO:0000313|Proteomes:UP000031100};
RA   Fomenkov A., Lunnen K.D., Zhu Z., Wilson G.G., Vincze T.,
RA   Roberts R.J.;
RT   "Complete Genome Sequence and Methylome Analysis of Bacillus sp.
RT   X1(2014).";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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; CP008855; AIM16560.1; -; Genomic_DNA.
DR   RefSeq; WP_038538164.1; NZ_CP008855.1.
DR   EnsemblBacteria; AIM16560; AIM16560; HW35_09970.
DR   KEGG; gst:HW35_09970; -.
DR   PATRIC; fig|1565991.4.peg.2012; -.
DR   KO; K02313; -.
DR   Proteomes; UP000031100; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000031100};
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:UP000031100}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      425    448       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   448 AA;  50922 MW;  FC65BC86FD2B4BF5 CRC64;
     MENIADLWHA ALAKIEKKIS KPSFDTWLKS TKAHSLQGDL LVITAPNEFA RDWLEERYSK
     LISGILYDIT GEELSVKFII PQNQKEEEFD IPTPPKKVKK DDDHIEFPSN ILNSKYTFDT
     FVIGSGNRFA HAASLAVAEA PAKAYNPLFI YGGVGLGKTH LMHAIGHYVL DHNPSAKVVY
     LSSEKFTNEF INSIRDNRAE SFRNKYRNVD VLLIDDIQFL AGKESTQEEF FHTFNSLHEE
     SKQIVISSDR PPREIPTLED RLRSRFEWGL ITDITPPDLE TRIAILRKKA KAEGLDIPNE
     VMLYIANQID SNIRELEGAL IRVVAYSSLI NKDINADLAA EALKDIIPSS KPKVITIHDI
     QKAVGELFNV KLEDFKAKKR TKSIAFPRQI AMYLSRELTD YSLPKIGEEF GGRDHTTVIH
     AHEKISKLLQ SDAQLQKQLK ELNEMLKI
//
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