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Database: UniProt
Entry: A4W4R1_ENT38
LinkDB: A4W4R1_ENT38
Original site: A4W4R1_ENT38 
ID   A4W4R1_ENT38            Unreviewed;       483 AA.
AC   A4W4R1;
DT   29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   29-MAY-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=Ent638_0001 {ECO:0000313|EMBL:ABP58691.1};
OS   Enterobacter sp. (strain 638).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Enterobacter.
OX   NCBI_TaxID=399742 {ECO:0000313|EMBL:ABP58691.1, ECO:0000313|Proteomes:UP000000230};
RN   [1] {ECO:0000313|Proteomes:UP000000230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=638 {ECO:0000313|Proteomes:UP000000230};
RX   PubMed=20485560; DOI=10.1371/journal.pgen.1000943;
RA   Taghavi S., van der Lelie D., Hoffman A., Zhang Y.B., Walla M.D.,
RA   Vangronsveld J., Newman L., Monchy S.;
RT   "Genome sequence of the plant growth promoting endophytic bacterium
RT   Enterobacter sp. 638.";
RL   PLoS Genet. 6:E1000943-E1000943(2010).
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; CP000653; ABP58691.1; -; Genomic_DNA.
DR   ProteinModelPortal; A4W4R1; -.
DR   STRING; 399742.Ent638_0001; -.
DR   EnsemblBacteria; ABP58691; ABP58691; Ent638_0001.
DR   KEGG; ent:Ent638_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000000230; 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   Complete proteome {ECO:0000313|Proteomes:UP000000230};
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:UP000000230}.
FT   DOMAIN      180    382       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}.
SQ   SEQUENCE   483 AA;  54562 MW;  A405ECD549BB8C17 CRC64;
     MPTITIIQCL SFIVRVESAV SLSLWQQCLA RLQDELPATE FSMWIRPLQA ELSDNTLALY
     APNRFVLDWV RDKYLNNING LLNDFCGADA PQLRFEVGTK PVTQTVRETV NVAAPAQIHV
     PTPRIIQPAR SGWDNVPAPA EPTYRSNVNV KHTFDNFVEG KSNQLARAAA RQVADNPGGA
     YNPLFLYGGT GLGKTHLLHA VGNGIVARKP NAKVVYMHSE RFVQDMVKAL QNNAIEEFKR
     YYRSVDALLI DDIQFFANKE RSQEEFFHTF NALLEGNQQI ILTSDRYPKE INGVEDRLKS
     RFGWGLTVAI EPPELETRVA ILMKKADEND IRLPGEVAFF IAKRLRSNVR ELEGALNRVI
     ANANFTGRAI TIDFVREALR DLLALQEKLV TIDNIQKTVA EYYKIKIADL LSKRRSRSVA
     RPRQMAMALA KELTNHSLPE IGDAFGGRDH TTVLHACRKI EQLREESHDI KEDFSNLIRT
     LSS
//
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