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Database: UniProt
Entry: A6CPN1_9BACI
LinkDB: A6CPN1_9BACI
Original site: A6CPN1_9BACI 
ID   A6CPN1_9BACI            Unreviewed;       448 AA.
AC   A6CPN1;
DT   24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2007, sequence version 1.
DT   25-OCT-2017, entry version 63.
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:EDL64153.1};
GN   ORFNames=BSG1_10804 {ECO:0000313|EMBL:EDL64153.1};
OS   Bacillus sp. SG-1.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=161544 {ECO:0000313|EMBL:EDL64153.1, ECO:0000313|Proteomes:UP000004417};
RN   [1] {ECO:0000313|EMBL:EDL64153.1, ECO:0000313|Proteomes:UP000004417}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG-1 {ECO:0000313|EMBL:EDL64153.1,
RC   ECO:0000313|Proteomes:UP000004417};
RA   Tebo B., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (JUN-2007) 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}.
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:EDL64153.1}.
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DR   EMBL; ABCF01000027; EDL64153.1; -; Genomic_DNA.
DR   RefSeq; WP_006837291.1; NZ_ABCF01000027.1.
DR   ProteinModelPortal; A6CPN1; -.
DR   EnsemblBacteria; EDL64153; EDL64153; BSG1_10804.
DR   Proteomes; UP000004417; 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: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:UP000004417};
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:UP000004417}.
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;  50893 MW;  7F6D4350F87ADEED CRC64;
     MENIGDLWNK ALSNIEKKIS KPSFDTWLKS TKAHSIQGDT LVITAPNEFA RDWLEGRYSQ
     LISDVLLEIT GEELIVKFII PQNQEPEEFD IPVPPKKVVD NDDGQEFQQN MLNPKYMFDT
     FVIGSGNRFA HAASLAVAEA PAKAYNPLFI YGGVGLGKTH LMHAIGHYVL EHNPAAKVVY
     LSSEKFTNEF INSIRDNKAV DFRNKYRNVD VLLIDDIQFL AGKEQTQEEF FHTFNTLHEE
     SKQIVISSDR PPKEIPTLED RLRSRFEWGL ITDITPPDLE TRIAILRKKA KAEGLDIPNE
     AMLYIANQID SNIRELEGAL IRVVAYSSLI NKDINADLAA EALKDIIPSS KPKVITIADI
     QRVVGEQFNV RMEDFKAKKR TKSIAFPRQI AMYLSREMTD FSLPKIGEEF GGRDHTTVIH
     AHEKISKMLG SDSTFQHQLK EIRDLLKN
//
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