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Database: UniProt
Entry: K4R888_9ACTN
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ID   K4R888_9ACTN            Unreviewed;       638 AA.
AC   K4R888;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   05-JUL-2017, entry version 40.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:CCK28904.1};
GN   ORFNames=BN159_4525 {ECO:0000313|EMBL:CCK28904.1};
OS   Streptomyces davawensis JCM 4913.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1214101 {ECO:0000313|EMBL:CCK28904.1, ECO:0000313|Proteomes:UP000008043};
RN   [1] {ECO:0000313|EMBL:CCK28904.1, ECO:0000313|Proteomes:UP000008043}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 4913 {ECO:0000313|EMBL:CCK28904.1,
RC   ECO:0000313|Proteomes:UP000008043};
RX   PubMed=23043000; DOI=10.1128/JB.01592-12;
RA   Jankowitsch F., Schwarz J., Ruckert C., Gust B., Szczepanowski R.,
RA   Blom J., Pelzer S., Kalinowski J., Mack M.;
RT   "Genome Sequence of the Bacterium Streptomyces davawensis JCM 4913 and
RT   Heterologous Production of the Unique Antibiotic Roseoflavin.";
RL   J. Bacteriol. 194:6818-6827(2012).
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:SAAS00731907}.
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; HE971709; CCK28904.1; -; Genomic_DNA.
DR   RefSeq; WP_015659251.1; NC_020504.1.
DR   EnsemblBacteria; CCK28904; CCK28904; BN159_4525.
DR   GeneID; 31226513; -.
DR   KEGG; sdv:BN159_4525; -.
DR   PATRIC; fig|1214101.3.peg.4581; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000008043; 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; 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   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:UP000008043};
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:UP000008043}.
FT   DOMAIN      331    459       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      545    614       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     339    346       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   638 AA;  70674 MW;  7C0AED6BA0C66C1D CRC64;
     MADVPADLAA VWPRVLEQLL GEGRGQGVEA KDEHWIRRCQ PLALVADTAL LAVPNEFAKG
     VLEGRLAPIV SETLSRECGR PIRIAITVDD SAGEPPAPPA PPARPQPRYE EPELPSGPYE
     GYGRHRGADG DAYPSRPDQG DQLPTARPAY PSEYQRPEPG AWPRPQQDEY SWQQQRLGFP
     ERDPYASPSQ DSYGQPPQDY RPQSMDRPSY EGQRADYDGQ RPDYDSPRGD YDKPRGDYDG
     GRPNYDQRDA RRDLPEPSTG PAHRSGPAAP ALPSASGAPG PLAAQPAPAT GPGEPTARLN
     PKYLFDTFVI GASNRFAHAA AVAVAEAPAK AYNPLFIYGE SGLGKTHLLH AIGHYARSLY
     PGTRVRYVSS EEFTNEFINS IRDGKGDSFR KRYREMDILL VDDIQFLADK ESTQEEFFHT
     FNTLHNANKQ IVLSSDRPPK QLVTLEDRLR NRFEWGLITD VQPPELETRI AILRKKAVQE
     QLNAPPEVLE FIASRISRNI RELEGALIRV TAFASLNRQP VDLGLTEIVL KDLIPGGDDS
     APEITSTAIM SATADYFGLT VEDLCGTSRG RALVTARQIA MYLCRELTDL SLPKIGALFG
     GRDHTTVMHA DRKIRNLMAE RRSIYNQVTE LTNRIKNG
//
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