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Database: UniProt
Entry: D9XNU3_9ACTN
LinkDB: D9XNU3_9ACTN
Original site: D9XNU3_9ACTN 
ID   D9XNU3_9ACTN            Unreviewed;       652 AA.
AC   D9XNU3;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, 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   ORFNames=SSRG_03181 {ECO:0000313|EMBL:EFL40377.1};
OS   Streptomyces griseoflavus Tu4000.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=467200 {ECO:0000313|EMBL:EFL40377.1, ECO:0000313|Proteomes:UP000002968};
RN   [1] {ECO:0000313|EMBL:EFL40377.1, ECO:0000313|Proteomes:UP000002968}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tu4000 {ECO:0000313|EMBL:EFL40377.1,
RC   ECO:0000313|Proteomes:UP000002968};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA   Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA   Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA   Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA   Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA   Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Thomson T., Walk T., White J., Yandava C., Straight P.,
RA   Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA   Wieland-Brown L.C., Haas B., Nusbaum C., Birren B.;
RT   "Annotation of Streptomyces griseoflavus strain Tu4000.";
RL   Submitted (FEB-2009) 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}.
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DR   EMBL; GG657758; EFL40377.1; -; Genomic_DNA.
DR   STRING; 467200.SSRG_03181; -.
DR   EnsemblBacteria; EFL40377; EFL40377; SSRG_03181.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002968; 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:UP000002968};
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:UP000002968}.
FT   DOMAIN      345    473       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      559    628       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     353    360       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   652 AA;  72792 MW;  A2D57F3A40E6961F CRC64;
     MADVPADLAA VWPRVLEQLL GEGRGQGVEG KDEHWIRRCQ PLALVADTAL LAVPNEFAKG
     VLEGRLAPVV SETLSRECGR PIRIAITVDD TVGEPSPPPV PRPQPRYEEP ELPPGRQDRP
     DRPDRLERQD RQDRQDREPY ETYDGYDGYG RRRADQHSGD QLPTARPAYP SEYQRPEPGS
     WPRPGQEEYG WQQQRLGFPE RDPYASPPQD GAYGSPDSYG SQDGYGGSPA QDYRPQPMDR
     PPYDQQRSDY EPSRGDYDQR DARRRELPEP PPGSGHVHRG GPVGPNLPTT GAPGPLAAQP
     APATGPGEPT ARLNPKYLFD TFVIGASNRF AHAAAVAVAE APAKAYNPLF IYGESGLGKT
     HLLHAIGHYA RSLYPGTRVR YVSSEEFTNE FINSIRDGKG DSFRKRYREM DILLVDDIQF
     LADKESTQEE FFHTFNTLHN ANKQIVLSSD RPPKQLVTLE DRLRNRFEWG LITDVQPPEL
     ETRIAILRKK AVQEQLNAPP EVLEFIASRI SRNIRELEGA LIRVTAFASL NRQPVDLGLT
     EIVLKDLMPG GDDSTPEITS TAIMGATADY FGLTVEDLCG SSRGRQLVTA RQIAMYLCRE
     LTDLSLPKIG ALFGGRDHTT VMHADRKIRN LMAERRSIYN QVTELTNRIK AG
//
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