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Database: UniProt
Entry: B1VDX2_CORU7
LinkDB: B1VDX2_CORU7
Original site: B1VDX2_CORU7 
ID   B1VDX2_CORU7            Unreviewed;       586 AA.
AC   B1VDX2;
DT   20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT   20-MAY-2008, sequence version 1.
DT   27-SEP-2017, entry version 79.
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   OrderedLocusNames=cu0001 {ECO:0000313|EMBL:CAQ03961.1};
OS   Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=504474 {ECO:0000313|EMBL:CAQ03961.1, ECO:0000313|Proteomes:UP000001727};
RN   [1] {ECO:0000313|EMBL:CAQ03961.1, ECO:0000313|Proteomes:UP000001727}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43042 / DSM 7109 {ECO:0000313|Proteomes:UP000001727};
RX   PubMed=18367281; DOI=10.1016/j.jbiotec.2008.02.009;
RA   Tauch A., Trost E., Tilker A., Ludewig U., Schneiker S., Goesmann A.,
RA   Arnold W., Bekel T., Brinkrolf K., Brune I., Goetker S.,
RA   Kalinowski J., Kamp P.-B., Lobo F.P., Viehoever P., Weisshaar B.,
RA   Soriano F., Droege M., Puehler A.;
RT   "The lifestyle of Corynebacterium urealyticum derived from its
RT   complete genome sequence established by pyrosequencing.";
RL   J. Biotechnol. 136:11-21(2008).
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:SAAS00731907}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00756131}.
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; AM942444; CAQ03961.1; -; Genomic_DNA.
DR   RefSeq; WP_012359267.1; NC_010545.1.
DR   ProteinModelPortal; B1VDX2; -.
DR   STRING; 504474.cur_0001; -.
DR   EnsemblBacteria; CAQ03961; CAQ03961; cu0001.
DR   KEGG; cur:cu0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; AGKEHTQ; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000001727; 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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001727};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00756112};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756124};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001727}.
FT   DOMAIN      279    407       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      490    559       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     287    294       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   586 AA;  64582 MW;  D6E746E46123DE2B CRC64;
     MSLTVTPDPR REEKGSRMTH APDPADPTKF ATIWHGLVDA WIEGDGTQFP PLSASSRSVL
     RQIQPVLFIN GIAVMTTPNE WSKGVVEGAL AEPIERVLGD ILQSPVTLSL SIREAEPEDT
     AQPTNTNTVP GAAEQQAPAG HSAVHTPARS TPAAHSTTAP APATPTAAEA RAPQSTAPSQ
     PSAPAESPQH DPKQDEHTRI LAAERLAQQH QGVNQPESRN EAFVPAEASS SPTADTDEGD
     RDSDTLLNKK YTFESFVIGG SNQFAHAACR AVAEAPARAY NPLFIWGESG LGKTHLLHAI
     GHYAKELQPD MRVRYVSSEE LTNDFINSIA NDRREEFKRE YRNLDMLIVD DIQFLQGKES
     TQEEFFHTFN ALHQANKQIV LSSDRPPRQL TTLEDRLRTR FEGGLITDVQ TPDLETRMAI
     LSRKAAAEGT TLPEDVLELI ASRYETSIRE LEGALIRVTA YCSLGKEPIT KQAAEIALRD
     IMPVDDVQMT PQVIIDVVSS YFDLTVDELV GKGRTKRFVQ ARQIAMYLCR ELTDLSLPKL
     GQAFGGRDHT TVMHAERRIR EQLTEDRVTF NEVQELTQRA KAAARG
//
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