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Database: UniProt
Entry: G2G738_9ACTN
LinkDB: G2G738_9ACTN
Original site: G2G738_9ACTN 
ID   G2G738_9ACTN            Unreviewed;       629 AA.
AC   G2G738;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   25-OCT-2017, entry version 43.
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:EGX60751.1};
GN   ORFNames=SZN_06499 {ECO:0000313|EMBL:EGX60751.1};
OS   Streptomyces zinciresistens K42.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=700597 {ECO:0000313|EMBL:EGX60751.1, ECO:0000313|Proteomes:UP000004217};
RN   [1] {ECO:0000313|EMBL:EGX60751.1, ECO:0000313|Proteomes:UP000004217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K42 {ECO:0000313|EMBL:EGX60751.1,
RC   ECO:0000313|Proteomes:UP000004217};
RA   Lin Y., Hao X., Johnstone L., Miller S.J., Wei G., Rensing C.;
RL   Submitted (AUG-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: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   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:EGX60751.1}.
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DR   EMBL; AGBF01000011; EGX60751.1; -; Genomic_DNA.
DR   EnsemblBacteria; EGX60751; EGX60751; SZN_06499.
DR   PATRIC; fig|700597.3.peg.1262; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004217; 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; 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   Complete proteome {ECO:0000313|Proteomes:UP000004217};
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:UP000004217}.
FT   DOMAIN      322    450       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      536    605       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     330    337       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   629 AA;  70032 MW;  C8E07475C7C104D6 CRC64;
     MWPRVLEQLL GEGRGQGVEV KDEHWIRRCQ PLALVADTAL LAVPNEFAKG VLEGRLAPVV
     SETLSRECGR PIRIAITVDD SAGEPPPPAP QPSAPFEQQG RPSSQHHYEE PELPSYEGYG
     RHRAEDQQRG PSNDPLPTAR PAYPGEYQRP EHAPGSWPRA SQDDYGWQQQ RLGFPERDPY
     ASPSQEPFSQ NPYPQDSYGP PSQDYRPQPR ERSSYDGHRP DYEQRRPDYD KPRGDYDQGG
     RRDLPDPPAG SGHVHRGGPV GANLPTTGAP GPLAAQPAPA SGPGEPTARL NPKYLFDTFV
     IGASNRFAHA AAVAVAEAPA KAYNPLFIYG ESGLGKTHLL HAIGHYARSL YPGTRVRYVS
     SEEFTNEFIN SIRDGKGDSF RKRYREMDIL LVDDIQFLAD KESTQEEFFH TFNTLHNANK
     QIVLSSDRPP KQLVTLEDRL RNRFEWGLIT DVQPPELETR IAILRKKAVQ EQLNAPPEVL
     EFIASRISRN IRELEGALIR VTAFASLNRQ PVDLGLTEIV LKDLIPGGED SAPEITSTAI
     MGATADYFGL TVEDLCGTSR GRALVTARQI AMYLCRELTD LSLPKIGALF GGRDHTTVMH
     ADRKIRNLMA ERRSIYNQVT ELTNRIKNG
//
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