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Database: UniProt
Entry: R4L8A8_9ACTN
LinkDB: R4L8A8_9ACTN
Original site: R4L8A8_9ACTN 
ID   R4L8A8_9ACTN            Unreviewed;       613 AA.
AC   R4L8A8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   05-JUL-2017, entry version 33.
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:AGL13511.1};
GN   ORFNames=L083_0001 {ECO:0000313|EMBL:AGL13511.1};
OS   Actinoplanes sp. N902-109.
OC   Bacteria; Actinobacteria; Micromonosporales; Micromonosporaceae;
OC   Actinoplanes.
OX   NCBI_TaxID=649831 {ECO:0000313|EMBL:AGL13511.1, ECO:0000313|Proteomes:UP000013541};
RN   [1] {ECO:0000313|EMBL:AGL13511.1, ECO:0000313|Proteomes:UP000013541}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N902-109 {ECO:0000313|EMBL:AGL13511.1,
RC   ECO:0000313|Proteomes:UP000013541};
RA   Hu H., Huang H., Lu X., Zhu B.;
RT   "Comparative analysis of rapamycin biosynthesis clusters between
RT   Streptomyces hygroscopicus ATCC 29253 and Actinoplanes sp. N902-109.";
RL   Submitted (MAY-2013) 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; CP005929; AGL13511.1; -; Genomic_DNA.
DR   EnsemblBacteria; AGL13511; AGL13511; L083_0001.
DR   KEGG; actn:L083_0001; -.
DR   PATRIC; fig|649831.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000013541; 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:UP000013541};
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:UP000013541}.
FT   DOMAIN      307    435       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      519    588       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     315    322       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   613 AA;  67496 MW;  707307C7C04DD1F3 CRC64;
     MSGGDGGGAA VADTVDLGGV WAAATDELAD EIASAQQRAY LRLTRLRAIV EDTALLSVPD
     TYTRDVIESR LRLAITEALS RRLGRPIQVA VTVRPPEDGS GRPGTVYGTP PPEPAAQPAA
     HYADPQPPVY PDRYPQAPVF DDGPTGSAQV PFAPGVPAAR DGFANEGFPG EGQDALFAAP
     LPMGQPEPPK STVAEEKPVE PPRQLPHYQD SPNDAGRGRM AAEPAQLRDN QRRPEERPRD
     DTLQMRHGGD NGPGRSPLGT QPAGARPGGN DGNRLNPKYM FETFVIGSSN RFAHAAAVAV
     AESPAKAYNP LFIYGSSGLG KTHLLHAIGH YATTLGHARS VRYVSTEEFT NDFINSLRDD
     KTQAFQRRYR DVDILLIDDI QFLENRERTQ EEFFHTFNTL HNANKQIVIS SDRSPRQLAT
     LEDRMRTRFE WGLLADIQPP DLETRIAILQ KKAAQERMYA PDDVLEFIAS RVSNSIRELE
     GALIRVTAFA SLTRSSVQLS LAEEVLRDFM PDGAGPEITA DQIMVSTADY FGVSLEDLRG
     HSRSRVLVNA RQVAMYLCRE LTDLSLPRIG QAFGGRDHTT VMHADRKIRQ HMAERRSLYN
     QIAELTNRIK QNT
//
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