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Database: UniProt
Entry: A0A0L8Q6Q5_9ACTN
LinkDB: A0A0L8Q6Q5_9ACTN
Original site: A0A0L8Q6Q5_9ACTN 
ID   A0A0L8Q6Q5_9ACTN        Unreviewed;       659 AA.
AC   A0A0L8Q6Q5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
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:KOG82899.1};
GN   ORFNames=ADK38_39000 {ECO:0000313|EMBL:KOG82899.1};
OS   Streptomyces varsoviensis.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=67373 {ECO:0000313|EMBL:KOG82899.1, ECO:0000313|Proteomes:UP000037020};
RN   [1] {ECO:0000313|Proteomes:UP000037020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-3589 {ECO:0000313|Proteomes:UP000037020};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-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: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:KOG82899.1}.
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DR   EMBL; LGUT01003689; KOG82899.1; -; Genomic_DNA.
DR   RefSeq; WP_030882167.1; NZ_JOFN01000011.1.
DR   EnsemblBacteria; KOG82899; KOG82899; ADK38_39000.
DR   PATRIC; fig|67373.7.peg.9047; -.
DR   Proteomes; UP000037020; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000037020};
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:UP000037020}.
FT   DOMAIN      352    480       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      566    635       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     360    367       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      635    659       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   659 AA;  73465 MW;  EF5BA1C322F6808A CRC64;
     MADLPADLAA VWPRVLEQLL GEGRGQGVEA KDERWITRCQ PLALVADTAL LAVPNEFAKG
     VLEGRLAPIV SETLSRECGR PIRIAITVDS TAGEPPAPQP PAPPHQQQHQ PHQERPQQQH
     YEEPPRDAYD GYDARESRDN YGRPASADDQ LPTARPAYPE YQQRPDPGAW PRPHDNYGWQ
     QPRLGGFPEN DPYAQPNQHQ ASQHNQHGQQ HPPQQYEQPY DKSYEKPYEQ TQYEPSQYDH
     QQPPSDYRSG VPERLPYDQQ QRRELHDVPP GHLRTGGQGG GQGGHQGGNG SALPAPTGAP
     GPLAAQPAPA PAPGEPHARL NPKYLFDTFV IGASNRFAHA AAVAVAEAPA KAYNPLFIYG
     ESGLGKTHLL HAIGHYARSL YPGTRVRYVS SEEFTNEFIN SIRDGKGDTF RKRYRDVDIL
     LVDDIQFLAS KESTQEEFFH TFNTLHNANK QIVLSSDRPP KQLVTLEDRL RNRFEWGLTT
     DVQPPELETR IAILRKKAVQ EQLNAPPEVL EFIASRISRN IRELEGALIR VTAFASLNRQ
     PVDLGLTEIV LKDLIPGGED AAPEITAPAI MAATADYFGH TVEDLCGASR SRVLVTARQI
     AMYLCRELTD LSLPKIGAQF GNRDHTTVMH ADRKIRALMA ERRSIYNQVT ELTNRIKNS
//
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