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Database: UniProt
Entry: DNAA_AZOVD
LinkDB: DNAA_AZOVD
Original site: DNAA_AZOVD 
ID   DNAA_AZOVD              Reviewed;         478 AA.
AC   C1DFU2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 58.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   Name=dnaA {ECO:0000255|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Avin_00010;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K.,
RA   Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J.,
RA   Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S.,
RA   O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J.,
RA   Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J.,
RA   Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R.,
RA   Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe
RT   specialized to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00377}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00377}.
DR   EMBL; CP001157; ACO76269.1; -; Genomic_DNA.
DR   RefSeq; WP_012698697.1; NC_012560.1.
DR   ProteinModelPortal; C1DFU2; -.
DR   SMR; C1DFU2; -.
DR   STRING; 322710.Avin_00010; -.
DR   EnsemblBacteria; ACO76269; ACO76269; Avin_00010.
DR   KEGG; avn:Avin_00010; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; AVIN322710:G1GCS-1-MONOMER; -.
DR   Proteomes; UP000002424; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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; Complete proteome; Cytoplasm; DNA replication;
KW   DNA-binding; Nucleotide-binding.
FT   CHAIN         1    478       Chromosomal replication initiator protein
FT                                DnaA.
FT                                /FTId=PRO_1000205647.
FT   NP_BIND     183    190       ATP. {ECO:0000255|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   478 AA;  54007 MW;  6F54711ED849DD56 CRC64;
     MSVELWQQCV ELLRDELPAQ QFNTWIRPLQ VEADGDELRV YAPNRFVLDW VNEKYLGRLL
     ELLGERSEDV TPSVSLLIGS KRSSAPRAVQ PASPPPAVVQ AAPVAIEEAS AARTVDAQPV
     APATVRTERS VQVEGGLKHT SYLNRAFTFE NFVEGKSNQL ARAAAWQVAD NPKHGYNPLF
     LYGGVGLGKT HLMHAVGNHL LKKNPNAKVV YLHSERFVAD MVKALQLNAI NEFKRFYRSV
     DALLIDDIQF FAKKERSQEE FFHTFNALLE GGQQVILTSD RYPKEIEGLE ERLKSRFGWG
     LTVAVEPPEL ETRVAILMKK AEQTKVELPH DAAFFIAQRI RSNVRELEGA LKRVIAHSHF
     TNHPITIELI RESLKDLLAL QDKLVSIDNI QRTVAEYYKI KIADLLSKRR SRSVARPRQV
     AMALSKELTN HSLPEIGDSF GGRDHTTVLH ACRKIAELRE TDADIREDYK NLLRTLTT
//
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