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Database: UniProt
Entry: E0SNF6_DICD3
LinkDB: E0SNF6_DICD3
Original site: E0SNF6_DICD3 
ID   E0SNF6_DICD3            Unreviewed;       462 AA.
AC   E0SNF6;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   20-DEC-2017, entry version 55.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:ADN00707.1};
GN   OrderedLocusNames=Dda3937_01060 {ECO:0000313|EMBL:ADN00707.1};
OS   Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Dickeya.
OX   NCBI_TaxID=198628 {ECO:0000313|EMBL:ADN00707.1, ECO:0000313|Proteomes:UP000006859};
RN   [1] {ECO:0000313|EMBL:ADN00707.1, ECO:0000313|Proteomes:UP000006859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3937 {ECO:0000313|EMBL:ADN00707.1,
RC   ECO:0000313|Proteomes:UP000006859};
RX   PubMed=21217001; DOI=10.1128/JB.01513-10;
RA   Glasner J.D., Yang C.H., Reverchon S., Hugouvieux-Cotte-Pattat N.,
RA   Condemine G., Bohin J.P., Van Gijsegem F., Yang S., Franza T.,
RA   Expert D., Plunkett G. III, San Francisco M.J., Charkowski A.O.,
RA   Py B., Bell K., Rauscher L., Rodriguez-Palenzuela P., Toussaint A.,
RA   Holeva M.C., He S.Y., Douet V., Boccara M., Blanco C., Toth I.,
RA   Anderson B.D., Biehl B.S., Mau B., Flynn S.M., Barras F.,
RA   Lindeberg M., Birch P.R., Tsuyumu S., Shi X., Hibbing M., Yap M.N.,
RA   Carpentier M., Dassa E., Umehara M., Kim J.F., Rusch M., Soni P.,
RA   Mayhew G.F., Fouts D.E., Gill S.R., Blattner F.R., Keen N.T.,
RA   Perna N.T.;
RT   "Genome sequence of the plant-pathogenic bacterium Dickeya dadantii
RT   3937.";
RL   J. Bacteriol. 193:2076-2077(2011).
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:SAAS00724167}.
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; CP002038; ADN00707.1; -; Genomic_DNA.
DR   STRING; 198628.Dda3937_01060; -.
DR   EnsemblBacteria; ADN00707; ADN00707; Dda3937_01060.
DR   KEGG; ddd:Dda3937_01060; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006859; Chromosome.
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; IPR024633; DnaA_N_dom.
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   Pfam; PF11638; DnaA_N; 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:UP000006859};
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   ECO:0000313|EMBL:ADN00707.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006859}.
FT   DOMAIN      159    361       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      370    439       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      321    341       {ECO:0000256|SAM:Coils}.
FT   COILED      439    459       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   462 AA;  52095 MW;  4730B2B84FE64FF2 CRC64;
     MSLSLWQQCL ARLQDELPAT EFSMWIRPLQ AELSDNTLAL YAPNRFVLDW VRDKYINNIN
     GLLNDFCGMD APLLRFEVGS KPMTPAVVST GHHSAAAPAP QARAASPVRP SWETPAAQAE
     HTYRSNVNPK HTFDNFVEGK SNQLARAAAR QVADNPGGAY NPLFLYGGTG LGKTHLLHAV
     GNGIIARKPN AKVVYMHSER FVQDMVKALQ NNAIEEFKRY YRSVDALLID DIQFFANKER
     SQEEFFHTFN ALLEGNQQII LTSDRYPKEI NGVEDRLKSR FGWGLTVAIE PPELETRVAI
     LMKKADENDI RLPGEVAFFI AKRLRSNVRE LEGALNRVIA NANFTGRSIT IDFVREALRD
     LLALQEKLVT IDNIQKTVAE YYKIKVADLL SKRRSRSVAR PRQMAMALAK ELTNHSLPEI
     GDAFGGRDHT TVLHACRKIE QLREESHDIK EDFSNLIRTL SS
//
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