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Database: UniProt
Entry: A0A0A3HS87_9BACI
LinkDB: A0A0A3HS87_9BACI
Original site: A0A0A3HS87_9BACI 
ID   A0A0A3HS87_9BACI        Unreviewed;       448 AA.
AC   A0A0A3HS87;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-SEP-2017, entry version 23.
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=CD33_12115 {ECO:0000313|EMBL:KGR75456.1};
OS   Lysinibacillus sinduriensis BLB-1 = JCM 15800.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Lysinibacillus.
OX   NCBI_TaxID=1384057 {ECO:0000313|EMBL:KGR75456.1, ECO:0000313|Proteomes:UP000030408};
RN   [1] {ECO:0000313|EMBL:KGR75456.1, ECO:0000313|Proteomes:UP000030408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15800 {ECO:0000313|EMBL:KGR75456.1,
RC   ECO:0000313|Proteomes:UP000030408};
RA   Zhang F., Wang G., Zhang L.;
RT   "Draft genome sequence of Lysinibacillus sinduriensis JCM 15800.";
RL   Submitted (FEB-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: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:KGR75456.1}.
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DR   EMBL; JPVO01000051; KGR75456.1; -; Genomic_DNA.
DR   RefSeq; WP_036200975.1; NZ_JPVO01000051.1.
DR   EnsemblBacteria; KGR75456; KGR75456; CD33_12115.
DR   Proteomes; UP000030408; 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   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:UP000030408};
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:UP000030408}.
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}.
SQ   SEQUENCE   448 AA;  50661 MW;  C4D3010727572D45 CRC64;
     MEHLEELWKN VLAQVEQKIS KPSFETWLKA TKLLSYKGST VTIAAPNSFA RDWLENHYVH
     LIAGILSELT GEDLLIKFVV QKDQDDDSLD LPVPVIQSKN DDEHAEITPG MLNPKYTFDT
     FVIGAGNRFA HAASLAVAEA PAKAYNPFFI YGGVGLGKTH LMHAIGHYVL EHNPNAKVVY
     LSSEKFTNEF INSIRDNKAV DFRNKYRNVD VLLIDDIQFL AGKESTQEEF FHTFNTLHTE
     SKQIVISSDR PPKEIPTLED RLRSRFEWGL ITDITPPDLE TRIAILRKKA KADGLNIPNE
     VMHYIANQID TNIRELEGAL IRVVAYSSLV NQDISTDLAA AALKDIIPNA KPRMITILDI
     QTAVGEHFNI KLEDFTAKRR TKSIAFPRQV AMYLSRELTD FSLPKIGDEF GGRDHTTVIH
     AHEKIVKLLK EDQLLQQDIK QIRSVLGK
//
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