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Database: UniProt
Entry: A0A0A1MKF8_9BACI
LinkDB: A0A0A1MKF8_9BACI
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ID   A0A0A1MKF8_9BACI        Unreviewed;       447 AA.
AC   A0A0A1MKF8;
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_1 {ECO:0000313|EMBL:CEI80294.1};
GN   Synonyms=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=BN997_00097 {ECO:0000313|EMBL:CEI80294.1};
OS   Oceanobacillus oncorhynchi.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Oceanobacillus.
OX   NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI80294.1, ECO:0000313|Proteomes:UP000040453};
RN   [1] {ECO:0000313|EMBL:CEI80294.1, ECO:0000313|Proteomes:UP000040453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Oc5 {ECO:0000313|EMBL:CEI80294.1,
RC   ECO:0000313|Proteomes:UP000040453};
RA   Urmite Genomes Urmite Genomes;
RL   Submitted (NOV-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}.
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DR   EMBL; CDGG01000001; CEI80294.1; -; Genomic_DNA.
DR   RefSeq; WP_042528650.1; NZ_CDGG01000001.1.
DR   EnsemblBacteria; CEI80294; CEI80294; BN997_00097.
DR   Proteomes; UP000040453; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000040453};
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:UP000040453}.
FT   DOMAIN      142    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      423    447       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   447 AA;  50740 MW;  BB65D72A6DA0D2DD CRC64;
     MENIEELWDA TLDIIKEKLS KPSFDTWLKN TKALHLEKNT LVISAPNEFT KDWLETQYTD
     LITQTLEKTT GTSLNAKFII PDSVEEPSDQ KPMPKPNIDA KTTDSPKSML NDKYTFDTFV
     IGAGNRFAHA ASLAVAEAPA KAYNPLFIYG GVGLGKTHLM HAIGHYVREH NKDAKVVYLT
     SEKFTNEFIN AIMDNKSNHF RNKYRNIDVL LIDDIQFIAG KESTQEEFFH TFNALHEESK
     QIIISSDRPP KEIPTLEDRL RSRFEWGLIT DITPPDLETR IAILNKKAKA EGLDIPNEVM
     LYIANQINTN IRELEGALIR VVAYSSLVNQ DIDASLAANA LKDIIPSNKP KEITIPAIQE
     VVADRYHIRL EDFPAKKRTK SIAFPRQIAM YLSRELTDSS LPKIGQEFGG RDHTTVIHAH
     EKISKLLETD TELDRDIEEL KEKLKSL
//
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