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Database: UniProt
Entry: G8WWW8_STREN
LinkDB: G8WWW8_STREN
Original site: G8WWW8_STREN 
ID   G8WWW8_STREN            Unreviewed;       617 AA.
AC   G8WWW8;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   05-JUL-2017, entry version 41.
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   OrderedLocusNames=SCATT_31110 {ECO:0000313|EMBL:AEW95482.1};
OS   Streptomyces cattleya (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC
OS   14057 / NRRL 8057).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1003195 {ECO:0000313|EMBL:AEW95482.1, ECO:0000313|Proteomes:UP000007842};
RN   [1] {ECO:0000313|Proteomes:UP000007842}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057
RC   {ECO:0000313|Proteomes:UP000007842};
RA   Ou H.-Y., Li P., Zhao C., O'Hagan D., Deng Z.;
RT   "Complete genome sequence of Streptomyces cattleya strain DSM 46488.";
RL   Submitted (DEC-2011) 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: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; CP003219; AEW95482.1; -; Genomic_DNA.
DR   STRING; 1003195.SCAT_3117; -.
DR   EnsemblBacteria; AEW95482; AEW95482; SCATT_31110.
DR   KEGG; scy:SCATT_31110; -.
DR   PATRIC; fig|1003195.29.peg.3107; -.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; FPERDPY; -.
DR   Proteomes; UP000007842; 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:UP000007842};
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:UP000007842}.
FT   DOMAIN      311    439       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      525    594       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     319    326       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   617 AA;  67756 MW;  B23721EFB6B70005 CRC64;
     MADVTADLAA VWPRVLDHLL ADGQGVEAKD QRWLKACQAL ALVADTALLA APNEYAKGVL
     EGRLLPVITE GLTREFGRPI RIAITVDSST AAAAPQAPAA DRQPAPQQPP APAPGRYAEQ
     RRDYEDYPRS AEDGPVIRRA YPDYPSGHES GGWPPPAHSD PYAHGRPQEH GHGGPEGTDA
     WQQPRRGGYP DRDPYGGGQR DYGQQQEYGQ HGQQQEYTQQ EFGQPDYGQQ TGYPAPQPPE
     RPGGGVRPAD ALPASSGAPG PLAAQPAPAP GPGEPTARLN PKYLFDTFVI GASNRFAHAA
     AVAVAEAPAK AYNPLFIYGE SGLGKTHLLH AIGHYARSLY PGTRVRYVSS EEFTNEFINS
     IRDGKGDAFR KRYREMDILL VDDIQFLASK ESTQEEFFHT FNTLHNANKQ IVLSSDRPPK
     QLVTLEDRLR NRFEWGLITD VQPPELETRI AILRKKAVQE QLNAPPEVLE FIASRISRNI
     RELEGALIRV TAFASLNRQP VDLQLTEIVL KDLIPGGEDA VPEISGNAIM AETAAYFGLT
     VEDLCGSSRS RVLVTARQIA MYLCRELTDL SLPKIGALFG GRDHTTVMHA DRKIRALMAE
     RRSIYNQVTE LTNRIKS
//
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