GenomeNet

Database: UniProt
Entry: D9W2Z0_9ACTN
LinkDB: D9W2Z0_9ACTN
Original site: D9W2Z0_9ACTN 
ID   D9W2Z0_9ACTN            Unreviewed;       599 AA.
AC   D9W2Z0;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   20-DEC-2017, entry version 45.
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=SSNG_03536 {ECO:0000313|EMBL:EFL16284.1};
OS   Streptomyces sp. C.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL16284.1, ECO:0000313|Proteomes:UP000005763};
RN   [1] {ECO:0000313|EMBL:EFL16284.1, ECO:0000313|Proteomes:UP000005763}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C {ECO:0000313|EMBL:EFL16284.1,
RC   ECO:0000313|Proteomes:UP000005763};
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 sp. strain C.";
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; GG657750; EFL16284.1; -; Genomic_DNA.
DR   STRING; 253839.SSNG_03536; -.
DR   EnsemblBacteria; EFL16284; EFL16284; SSNG_03536.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005763; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000005763};
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:UP000005763}.
FT   DOMAIN      292    420       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      506    575       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     300    307       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      575    595       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   599 AA;  66351 MW;  E9E054CFEA3D8079 CRC64;
     MADVPADLAA VWPRVLEKLL GEGQQGIEPK DKQWVERCQP LALVADTALL AVPNEWGKRV
     LEGRLAPLIS DALSRECGRP IRIAITVDDS AGEPAPPAPP APSPREGYEP YGGQRPGAGE
     DQLPAARPAY PEYQQPRQEP GSWPRGGQDE YGWQQQRLGG FPERDPYATP QPGYLQQPEP
     GGYDQGGYES SSSYEPQKYE PQKYDSPSYE PQPYEPQGYE PQQYEQPSPR PAPGRPTPAP
     PPSAPSGGST SGPLEPTARL NPKYLFDTFV IGASNRFAHA AAVAVAEAPA KAYNPLFVYG
     ESGLGKTHLL HAIGHYARSL YPGTRVRYVS SEEFTNEFIN SIRDGKGDAF RKRYREMDIL
     LVDDIQFLAS KESTQEEFFH TFNTLHNANK QIVLSSDRPP KQLVTLEDRL RNRFEWGLIT
     DVQPPELETR IAILRKKAVQ EQLNAPPEVL EFIASRISRN IRELEGALIR VTAFASLNRQ
     PVDLGLTEDV LKNLIPGGED SAPEITASDI MAATADYFGL TVDDLCGSSR SRVLVTARQI
     AMYLCRELTD LSLPKIGAQF GGRDHTTVMH ADRKIRALMA ERRSIYNQVT ELTNRIKNG
//
DBGET integrated database retrieval system