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Database: UniProt
Entry: A0A0A8JFB8_BACSX
LinkDB: A0A0A8JFB8_BACSX
Original site: A0A0A8JFB8_BACSX 
ID   A0A0A8JFB8_BACSX        Unreviewed;       450 AA.
AC   A0A0A8JFB8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   05-JUL-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=OXB_0971 {ECO:0000313|EMBL:BAQ09443.1};
OS   Bacillus sp. (strain OxB-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=98228 {ECO:0000313|EMBL:BAQ09443.1, ECO:0000313|Proteomes:UP000031651};
RN   [1] {ECO:0000313|Proteomes:UP000031651}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OxB-1 {ECO:0000313|Proteomes:UP000031651};
RA   Yamaguchi T., Asano Y.;
RT   "Complete genome of an aldoxime degrader Bacillus sp. OxB-1.";
RL   Submitted (AUG-2013) 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}.
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DR   EMBL; AP013294; BAQ09443.1; -; Genomic_DNA.
DR   RefSeq; WP_041072396.1; NZ_AP013294.1.
DR   EnsemblBacteria; BAQ09443; BAQ09443; OXB_0971.
DR   KEGG; baco:OXB_0971; -.
DR   KO; K02313; -.
DR   Proteomes; UP000031651; Chromosome.
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:UP000031651};
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:UP000031651}.
FT   DOMAIN      144    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   450 AA;  50859 MW;  34075457CF470AF6 CRC64;
     MEHFEELWNE VLAKVEKKIS RPSFETWLKS TKLMSYGDEI VTIAAPNAFA QDWLENNYVH
     LITGILSELT GEDRIIQFYV PEDMESNEFA MPKPSVKPPV EKGPSMSSPA MLNMKYTFDT
     FVIGSGNRFA HAASLAVAEA PAKAYNPLFI YGGVGLGKTH LMHAIGHYVL EQNPSAKVVY
     LSSEKFTNEF INSIRDNKAV EFRNQYRNVD VLLIDDIQFL AGKEQTQEEF FHTFNTLHEE
     SKQIVISSDR PPKEIPTLED RLRSRFEWGL ITDIAPPDLE TRIAILRKKA KADGLIDIPN
     EVMLYIANQI DSNIRELEGA LIRVVAYSSL VNTDINIDLA AEALKDIIPN TRPRAVTILD
     IQKSVGEHFN VRLEDFTAKK RTRSIAFPRQ IAMFLSRELT DASLPKIGSE FGGRDHSTVI
     HAHEKISKML KDDEALQQDL QEIKNALGRG
//
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