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Database: UniProt
Entry: A0A0L0MDD1_9BURK
LinkDB: A0A0L0MDD1_9BURK
Original site: A0A0L0MDD1_9BURK 
ID   A0A0L0MDD1_9BURK        Unreviewed;       522 AA.
AC   A0A0L0MDD1;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ORFNames=BVER_05016 {ECO:0000313|EMBL:KND60275.1};
OS   Candidatus Burkholderia verschuerenii.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=242163 {ECO:0000313|EMBL:KND60275.1, ECO:0000313|Proteomes:UP000036959};
RN   [1] {ECO:0000313|Proteomes:UP000036959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot4 {ECO:0000313|Proteomes:UP000036959};
RA   Carlier A., Eberl L., Pinto-Carbo M.;
RT   "Comparative genomics of Burkholderia leaf nodule symbionts.";
RL   Submitted (JUN-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KND60275.1}.
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DR   EMBL; LFJJ01000072; KND60275.1; -; Genomic_DNA.
DR   RefSeq; WP_050453873.1; NZ_LFJJ01000072.1.
DR   EnsemblBacteria; KND60275; KND60275; BVER_05016.
DR   PATRIC; fig|242163.4.peg.6389; -.
DR   Proteomes; UP000036959; Unassembled WGS sequence.
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:UP000036959};
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:UP000036959}.
FT   DOMAIN      219    353       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      430    499       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     227    234       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   522 AA;  57595 MW;  86FA2CBE7D15FEB9 CRC64;
     MNDFWEHCSA LLERELTPQQ YVTWIKPLTP VDFDADANTL RIAAPNRFKL DWVKSQFSGR
     IADVAQDFFS APIDVQFVLD PKATARNAIG SGPNAAPRPS APAPAPRAPA PAAAVPQAPT
     VVAHANATAH INALAAEATQ QSQDDQADLD LPSLDANEAA AGRRTWRPGG APSAGGETDS
     AYERSKLNPV LTFDNFVTGK ANQLARAAAI QVADNPGISY NPLFLYGGVG LGKTHLIHAI
     GNQLLMDKAG ARIRYIHAEQ YVSDVVKAYQ RKAFDDFKRY YHSLDLLLID DIQFFSGKNR
     TQEEFFYAFE ALVANKAQVI ITSDTYPKEI SGIDDRLISR FDSGLTVAIE PPELEMRVAI
     LMRKALSEGV SLSEDVAFFV AKHLRSNVRE LEGALRKILA YSKFHGRDIT IELTKEALKD
     LLTVQNRQIS VENIQKTVAD FYNIKVADMY SKKRPANIAR PRQIAMYLAK ELTQKSLPEI
     GELFGGRDHT TVLHAVRKIA AERGNDAQLN HELHVLEQTL KG
//
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