GenomeNet

Database: UniProt
Entry: A0A0F7N4B9_9ACTN
LinkDB: A0A0F7N4B9_9ACTN
Original site: A0A0F7N4B9_9ACTN 
ID   A0A0F7N4B9_9ACTN        Unreviewed;       648 AA.
AC   A0A0F7N4B9;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 19.
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   ORFNames=AA958_16210 {ECO:0000313|EMBL:AKH83495.1};
OS   Streptomyces sp. CNQ-509.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=444103 {ECO:0000313|EMBL:AKH83495.1, ECO:0000313|Proteomes:UP000034283};
RN   [1] {ECO:0000313|EMBL:AKH83495.1, ECO:0000313|Proteomes:UP000034283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CNQ-509 {ECO:0000313|EMBL:AKH83495.1,
RC   ECO:0000313|Proteomes:UP000034283};
RA   Ruckert C., Albersmeier A., Leipoldt F., Winkler A., Zeyhle P.,
RA   Kalinowski J., Heide L., Kaysser L.;
RT   "Complete Genome Sequence of Streptomyces sp. CNQ-509, a Prolific
RT   Producer of Meroterpenoid Chemistry.";
RL   Submitted (MAY-2015) 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:SAAS00735475}.
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   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP011492; AKH83495.1; -; Genomic_DNA.
DR   RefSeq; WP_047016801.1; NZ_CP011492.1.
DR   EnsemblBacteria; AKH83495; AKH83495; AA958_16210.
DR   KEGG; strc:AA958_16210; -.
DR   PATRIC; fig|444103.5.peg.3415; -.
DR   KO; K02313; -.
DR   Proteomes; UP000034283; Chromosome.
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; 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   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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034283};
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:UP000034283}.
FT   DOMAIN      341    469       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      555    624       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     349    356       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      624    648       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   648 AA;  70000 MW;  A7409E54E461F118 CRC64;
     MADLPADLAA VWPRVLERLL ADEQGVEAKD HRWLRDCQPL VLVAGTAVLA VPNEYAKGVF
     EGRLASKITD ALSHACRQPI GLAVTVSPGE PESKPQQGPP AQPGPESGGH GPHVPHSPQA
     PQPPAHEQAA HPGAPHLPLP HTAAQPTHQS HQPPHQSHGG PLPEPPYDAY SRPAPGDDRL
     PTAAPTYPEY AQPRPAPAAW PRADHHPGPP GTQPDTSAGP DGTDFYPAHD HLAQRPAHDR
     YAHPGGHTGG HTGGHTGGHT GGHSPSGAPI PPLVQAMGNV ELPAPSGAPG PLAAQPAPAT
     GPGEPTARLN PKYLFDTFVI GASNRFAHAA AVAVAEAPAK AYNPLFIYGE SGLGKTHLLH
     AIGHYARSLY PGTRVRYVSS EEFTNEFINS IRDGKADTFR KRYRDMDILL VDDVQFLASK
     ESTQEEFFHT FNTLHNANKQ IVLSSDRPPK QLITLEDRLR NRFEWGLITD VQPPELETRI
     AILRKKAVQE QLNAPPEVLE FIASRISRNI RELEGALIRV TAFASLNRQP VDLGLTEIVL
     KDLIPGGEDT APEITAAAIM AATADYFGLT VEDLCGSSRS RVLVTARQIA MYLCRELTDL
     SLPKIGAQFG NRDHTTVMHA DRKIRALMAE RRSIYNQVTE LTNRIKNS
//
DBGET integrated database retrieval system