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Database: UniProt
Entry: A0A136IHY4_9BURK
LinkDB: A0A136IHY4_9BURK
Original site: A0A136IHY4_9BURK 
ID   A0A136IHY4_9BURK        Unreviewed;       516 AA.
AC   A0A136IHY4;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=BSCH_02673c {ECO:0000313|EMBL:KXJ67769.1};
OS   Candidatus Paraburkholderia schumannianae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1069530 {ECO:0000313|EMBL:KXJ67769.1};
RN   [1] {ECO:0000313|Proteomes:UP000053518}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UZHbot8 {ECO:0000313|Proteomes:UP000053518};
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:SAAS00756131}.
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:KXJ67769.1}.
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DR   EMBL; LFJH01000283; KXJ67769.1; -; Genomic_DNA.
DR   RefSeq; WP_062731822.1; NZ_LFJH01000283.1.
DR   EnsemblBacteria; KXJ67769; KXJ67769; BSCH_02673c.
DR   Proteomes; UP000053518; 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:SF12; PTHR30050:SF12; 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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000053518};
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:UP000053518}.
FT   DOMAIN      213    347       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      424    493       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     221    228       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   516 AA;  57002 MW;  17FEB2F4A23B609C CRC64;
     MNDFWEHCSA LLARELTPQQ YVTWIKPLTP VDFDAGANTL RIAAPNRFKL DWVKSQFSGR
     ITDVARDFFG APIDVQFVLD PKATARNAIG GGLNAAPRPT VSAPAAPQAS SVVAHANATA
     HINALAADAA QQSQAMQADQ ADLDLPSLDA NEAAAGRRTW RPGGAPSAAG ENDFAYERSK
     LNPVLTFDNF VTGKANQLAR AAAIQVADNP GISYNPLFLY GGVGLGKTHL IYAIGNQLLM
     DKAGARIRYI HAEQYVSDVV KAYQRKAFDD FKRYYHSLDL LLIDDIQFFS GKSRTQEEFF
     YAFEALVANK AQVIITSDTY PKEISGIDDR LISRFDSGLT VAIEPPELEM RVAILMRKAL
     SEGVSLSEDV AFFVAKHLRS NVRELEGALR KILAYSKFHG RDITIELTKE ALKDLLTVQN
     RQISVENIQK TVADFYNIKV ADMYSKKRPA NIARPRQIAM YLAKELTQKS LPEIGELFGG
     RDHTTVLHAV RKIASERGTD AQLNHELHVL EQTLKG
//
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