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Database: UniProt
Entry: A0A0R0EC30_9GAMM
LinkDB: A0A0R0EC30_9GAMM
Original site: A0A0R0EC30_9GAMM 
ID   A0A0R0EC30_9GAMM        Unreviewed;       441 AA.
AC   A0A0R0EC30;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   13-FEB-2019, entry version 25.
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=ABB34_00165 {ECO:0000313|EMBL:KRG88391.1};
OS   Stenotrophomonas daejeonensis.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas.
OX   NCBI_TaxID=659018 {ECO:0000313|EMBL:KRG88391.1, ECO:0000313|Proteomes:UP000050940};
RN   [1] {ECO:0000313|EMBL:KRG88391.1, ECO:0000313|Proteomes:UP000050940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 16244 {ECO:0000313|EMBL:KRG88391.1,
RC   ECO:0000313|Proteomes:UP000050940};
RA   Patil P.P., Midha S., Patil P.B.;
RT   "Genome sequencing and analysis of members of genus
RT   Stenotrophomonas.";
RL   Submitted (MAY-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: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   -!- 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:KRG88391.1}.
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DR   EMBL; LDJP01000002; KRG88391.1; -; Genomic_DNA.
DR   RefSeq; WP_057639220.1; NZ_LDJP01000002.1.
DR   EnsemblBacteria; KRG88391; KRG88391; ABB34_00165.
DR   PATRIC; fig|659018.3.peg.745; -.
DR   OrthoDB; 219876at2; -.
DR   BioCyc; GCF_001431505:ABB34_RS00165-MONOMER; -.
DR   Proteomes; UP000050940; 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   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:UP000050940};
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:UP000050940}.
FT   DOMAIN      138    269       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      349    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     146    153       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      300    320       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   441 AA;  49537 MW;  4F52DAD6B1DC367B CRC64;
     MDAWPRCIER LEAEFPPEDV HTWLKPLQAD HRVDSMVLYA PNAFIVEQVR ERYLPRIREL
     LSHFAGVAEV QLEIGSRPRV AEPTPAAVAG PAAPTAPVVP FNGNLDSHYT FANFVEGRSN
     QLGLAAAFQA AAKPGDRAHN PLLLYGGTGL GKTHLMLAAG NAMRQANPAA RVLYLRSEQF
     FSAMIRALQE KAMDQFKRQF QQVDALLIDD IQFFAGKDRT QEEFFHTFNA LFDGKQQIIL
     TCDRYPREVE GLEARLKSRL AWGLSVAIEP PDFETRAAIV LAKARERGAE IPDDVAYLIA
     KKMRSNVRDL EGALNTLAAR ANFTGRAITT EFAQETLRDL LRAQQQAISI PNIQKTVADY
     YGLQIKDLLS KRRTRSLARP RQVAMALTKE LTEHSLPEIG DAFAGRDHTT VLHACRQIRT
     LMETDGKLRE DWDKLIRKLS E
//
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