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Database: UniProt
Entry: A1WDT7_VEREI
LinkDB: A1WDT7_VEREI
Original site: A1WDT7_VEREI 
ID   A1WDT7_VEREI            Unreviewed;       483 AA.
AC   A1WDT7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   25-OCT-2017, entry version 87.
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   OrderedLocusNames=Veis_0001 {ECO:0000313|EMBL:ABM55794.1};
OS   Verminephrobacter eiseniae (strain EF01-2).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Verminephrobacter.
OX   NCBI_TaxID=391735 {ECO:0000313|EMBL:ABM55794.1, ECO:0000313|Proteomes:UP000000374};
RN   [1] {ECO:0000313|Proteomes:UP000000374}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EF01-2 {ECO:0000313|Proteomes:UP000000374};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O.,
RA   Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Stahl D.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Verminephrobacter eiseniae EF01-
RT   2.";
RL   Submitted (DEC-2006) 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: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; CP000542; ABM55794.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1WDT7; -.
DR   STRING; 391735.Veis_0001; -.
DR   EnsemblBacteria; ABM55794; ABM55794; Veis_0001.
DR   KEGG; vei:Veis_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000374; 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:UP000000374};
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:UP000000374}.
FT   DOMAIN      180    314       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      391    460       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     188    195       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      453    483       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   483 AA;  54008 MW;  FBBCB98BE40977F5 CRC64;
     MTEEFTHSPP PPLHWPGANA ADERSAGQGL WQACAEQLAR DLPEAQFNTW IKPLVAQVAQ
     DFSKITLLVG NRFKLDWIRA QYASQITALL GDLYGQPMAL ELALVPRESV ARTAHTPRPS
     ASGPPGAPGA ESASAGRDEA PQALRHRLNA ALTFETLVEG SANRMARSAG MHVAGMPGHL
     YNPLFVYGGV GLGKTHLVHA VGNRLLASRP QAKVLYVHAE QFVSDVVRSY QRRTFDEFKE
     RYHSLDLLLI DDVQFFANKD RTQEEFFNAF EALLTKKSHL VMTSDTYPKG LSNIHERLVS
     RFDSGLTVAI EPPELEMRVA ILINKAQAES TEMPEEVAFF VAKNVRSNVR ELEGALRKIL
     AYSRFNQKEI SIQLAREALR DLLSIQNRQI SVENIQKTVA DYYKIKVADM YSKKRPASIA
     RPRQIAMYLT KELTQKSLPE IGESFGGRDH TTVLHAVRKI AAERQQLTEL NQQLHVLEQT
     LKG
//
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