GenomeNet

Database: UniProt
Entry: A0A240TYZ5_9BURK
LinkDB: A0A240TYZ5_9BURK
Original site: A0A240TYZ5_9BURK 
ID   A0A240TYZ5_9BURK        Unreviewed;       471 AA.
AC   A0A240TYZ5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   13-FEB-2019, entry version 12.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=CBP34_00005 {ECO:0000313|EMBL:ART50367.1};
OS   Acidovorax carolinensis.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=553814 {ECO:0000313|EMBL:ART50367.1, ECO:0000313|Proteomes:UP000194432};
RN   [1] {ECO:0000313|EMBL:ART50367.1, ECO:0000313|Proteomes:UP000194432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NA3 {ECO:0000313|EMBL:ART50367.1};
RA   Singleton D.R., Lee J., Dickey A.N., Stroud A., Scholl E.H.,
RA   Wright F.A., Aitken M.D.;
RT   "Polyphasic characterization of four soil-derived phenanthrene-
RT   degrading Acidovorax strains and proposal of Acidovorax
RT   phenanthrenivorans sp. nov.";
RL   Submitted (MAY-2017) 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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP021361; ART50367.1; -; Genomic_DNA.
DR   KEGG; acin:CBP34_00005; -.
DR   KO; K02313; -.
DR   BioCyc; GCF_002157145:CBP34_RS00005-MONOMER; -.
DR   Proteomes; UP000194432; 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 {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000194432};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194432}.
FT   DOMAIN      168    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     176    183       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      448    468       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   471 AA;  52837 MW;  0EF9916158251DDB CRC64;
     MTEESHRSPM GPAGADAGQG LWQACVEQLA QDLPEQQFNT WIKPLVAQVA EDFSKVTLLV
     GNRFKLDWIR AQYAGRIAAL LESIYGQSVT LELALAQREA VARTYIRPAT TPTATPSDAP
     NHSSDEAPAG AFRTRLNPAL TFETLVEGTA NRMARSAAMH VAGMPGHLYN PLFIYGGVGL
     GKTHLVHAVG NKLLADRPDA KVLYIHAEQF VSDVVKAYQR RTFDEFKERY HSLDLLLIDD
     VQFFANKDRT QEEFFNAFEA LLAKKSHIVM TSDTYPKGLA NIHERLVSRF DSGLTVAIEP
     PELEMRVAIL INKARAESTE MPEEVAFFVA KNVRSNVREL EGALRKILAY SRFNQKEISI
     QLAREALRDL LSIQNRQISV ENIQKTVADY YKIKVADMYS KKRPASIARP RQIAMYLAKE
     LTQKSLPEIG ELFGGRDHTT VLHAVRKISG ERQQLTELNQ QLHVLEQTLK G
//
DBGET integrated database retrieval system