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Database: UniProt
Entry: L1KH37_9ACTN
LinkDB: L1KH37_9ACTN
Original site: L1KH37_9ACTN 
ID   L1KH37_9ACTN            Unreviewed;       679 AA.
AC   L1KH37;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   05-JUL-2017, entry version 35.
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:EKX60131.1};
GN   ORFNames=STRIP9103_04820 {ECO:0000313|EMBL:EKX60131.1};
OS   Streptomyces ipomoeae 91-03.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=698759 {ECO:0000313|EMBL:EKX60131.1, ECO:0000313|Proteomes:UP000010411};
RN   [1] {ECO:0000313|EMBL:EKX60131.1, ECO:0000313|Proteomes:UP000010411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=91-03 {ECO:0000313|EMBL:EKX60131.1,
RC   ECO:0000313|Proteomes:UP000010411};
RA   Huguet-Tapia J.C., Durkin A.S., Pettis G.S., Badger J.H.;
RL   Submitted (NOV-2012) 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}.
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:EKX60131.1}.
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DR   EMBL; AEJC01000675; EKX60131.1; -; Genomic_DNA.
DR   RefSeq; WP_009343295.1; NZ_AEJC01000675.1.
DR   EnsemblBacteria; EKX60131; EKX60131; STRIP9103_04820.
DR   PATRIC; fig|698759.3.peg.9140; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000010411; Unassembled WGS sequence.
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:UP000010411};
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:UP000010411}.
FT   DOMAIN      372    500       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      586    655       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     380    387       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   679 AA;  75434 MW;  206A3406B28AFE78 CRC64;
     MADVPADLAA VWPRVLEQLL GEGRGQGVEA KDEHWIKRCQ PLALVADTAL LAVPNEFAKG
     VLEGRLAPAV SQALSQECGR PIRIAITVDS SMGEPPPPVQ SQFEEPELPS APAQNRAPYD
     SRDTYDGQGR DVRDPYENPS TYENPSTYEN QNTYEGPRDP YEGYGRRGSD DRRTARGESL
     TGGAGDQLLP PRSDQFPAGR ADQLPTARPA YPSEYQRPEP GAWPRPSQDD YGWQQQRLGF
     PERDPYASPS ADYRPQSLDR PPYDQQRSEY DSARADYDQP RTDYDRPGGE YDQRPDRREL
     PEPSGGPGHA HRGGPAGSTS GPLASQPSPT PGPGEPTARL NPKYLFDTFV IGASNRFAHA
     AAVAVAEAPA KAYNPLFIYG ESGLGKTHLL HAIGHYARSL YPGTRVRYVS SEEFTNEFIN
     SIRDGKGDSF RKRYREMDIL LVDDIQFLAD KESTQEEFFH TFNTLHNANK QIVLSSDRPP
     KQLVTLEDRL RNRFEWGLIT DVQPPELETR IAILRKKAVQ EQLNAPPEVL EFIASRISRN
     IRELEGALIR VTAFASLNRQ PVDLGLTEIV LKDLIPGGEN ASPEITATAI MAATADYFGL
     TVDDLCGTSR GRALVTARQI AMYLCRELTD LSLPKIGAQF GNRDHTTVMH ADRKIRALMA
     ERRSIYNQVT ELTNRIKNG
//
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