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Database: UniProt
Entry: A0A0D7K6K6_9BURK
LinkDB: A0A0D7K6K6_9BURK
Original site: A0A0D7K6K6_9BURK 
ID   A0A0D7K6K6_9BURK        Unreviewed;       471 AA.
AC   A0A0D7K6K6;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-SEP-2017, entry version 21.
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=RP29_13855 {ECO:0000313|EMBL:KJA09940.1};
OS   Acidovorax temperans.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=80878 {ECO:0000313|EMBL:KJA09940.1, ECO:0000313|Proteomes:UP000032566};
RN   [1] {ECO:0000313|EMBL:KJA09940.1, ECO:0000313|Proteomes:UP000032566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KY4 {ECO:0000313|EMBL:KJA09940.1,
RC   ECO:0000313|Proteomes:UP000032566};
RA   Sheng K.-Y., Chin P.-S., Chan K.-G., Tan G.S.;
RT   "Isolation of bacteria from lake water.";
RL   Submitted (DEC-2014) 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:KJA09940.1}.
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DR   EMBL; JXYQ01000045; KJA09940.1; -; Genomic_DNA.
DR   EnsemblBacteria; KJA09940; KJA09940; RP29_13855.
DR   PATRIC; fig|80878.5.peg.2552; -.
DR   Proteomes; UP000032566; 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   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000032566};
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:UP000032566}.
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    471       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   471 AA;  52855 MW;  DA1B12D4F416E3B3 CRC64;
     MWQACVEQLA QDLPEQQFNT WIKPLVAQVA EDFSKVTLLV ANRFKLDWIR AQYAGRIAAL
     LEGLYGQPVT LELAIAQREA VTRTYVRPAS QPQDQRAAPS SSQAPDTTHG QGGQSAQGAS
     NGGSDDSSAG AFRNRLNPAL TFETLVEGTA NRMARSAAMH VAGMPGHLYN PLFIYGGVGL
     GKTHLVHAVG NRLLQDKPDA KILYIHAEQF VSDVVKAYQR RTFDEFKERY HSLDLLLIDD
     VQFFANKDRT QEEFFNAFEA LLAKKSHIVM TSDTYPKGLA NIHERLVSRF DSGLTVAIEP
     PELEMRVAIL INKARVEGTE MPEEVAFFVA KNVRSNVREL EGALRKILAY SRFNQKEISI
     QLAREALRDL LSIQNRQISV ENIQKTVADY YKIKVADMYS KKRPASIARP RQIAMYLAKE
     LTQKSLPEIG ELFGGRDHTT VLHAVRKISA ERQQLTELNQ QLHVLEQTLK G
//
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