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Database: UniProt
Entry: A0A0S2F3R1_9GAMM
LinkDB: A0A0S2F3R1_9GAMM
Original site: A0A0S2F3R1_9GAMM 
ID   A0A0S2F3R1_9GAMM        Unreviewed;       444 AA.
AC   A0A0S2F3R1;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   30-AUG-2017, entry version 15.
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   ECO:0000313|EMBL:ALN78163.1};
GN   ORFNames=LA76x_0001 {ECO:0000313|EMBL:ALN78163.1};
OS   Lysobacter antibioticus.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=84531 {ECO:0000313|EMBL:ALN78163.1, ECO:0000313|Proteomes:UP000060787};
RN   [1] {ECO:0000313|EMBL:ALN78163.1, ECO:0000313|Proteomes:UP000060787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=76 {ECO:0000313|EMBL:ALN78163.1,
RC   ECO:0000313|Proteomes:UP000060787};
RX   PubMed=26597042; DOI=10.1186/s12864-015-2191-z;
RA   de Bruijn I., Cheng X., de Jager V., Exposito R.G., Watrous J.,
RA   Patel N., Postma J., Dorrestein P.C., Kobayashi D., Raaijmakers J.M.;
RT   "Comparative genomics and metabolic profiling of the genus
RT   Lysobacter.";
RL   BMC Genomics 16:991-991(2015).
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}.
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DR   EMBL; CP011129; ALN78163.1; -; Genomic_DNA.
DR   RefSeq; WP_057916043.1; NZ_CP013141.1.
DR   EnsemblBacteria; ALN78163; ALN78163; LA76x_0001.
DR   KEGG; lab:LA76x_0001; -.
DR   KEGG; laq:GLA29479_1374; -.
DR   PATRIC; fig|84531.7.peg.1360; -.
DR   KO; K02313; -.
DR   Proteomes; UP000060787; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000060787};
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:UP000060787}.
FT   DOMAIN      141    272       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     149    156       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   444 AA;  50351 MW;  130AF0FA8D41E924 CRC64;
     MEAWPRCLER LEAEFPVEDV HTWLKPLQAT RRDDVTVLYA PNAFVVEHVR ERYLGRIREL
     LSYFAGSGEV SLEIGSLPRA VPAVARESEI AVSAPRPVAP PEPFQGNLDN HYTFDNFVEG
     RSNQLGRAAA WQAAQKPGER AHNPLLLYGG TGLGKTHLMF AAGNAMREAN PAMRVMYLRS
     EQFFSAMMKA LQDKTMDQFK RQFQRVDALL IDDIQFFAGK DRTQEEFFHT FNALFDGKQQ
     IILTCDRYPR EVEGLEPRLK SRLAWGLSVA IEPPDFETRA QIVISKAKER GAAVPEEVAF
     LLAKKMRSNV RDLEGALNTL TARANFTGRA ITTEFAQETL RDLLRAQQQA IGIPNIQKTV
     ADYYGLQIKD LLSKRRTRSL ARPRQVAMAL TKELTEHSLP EIGDAFAGRD HTTVLHACRQ
     IRTLMETDGK LREDWDKLIR KLSE
//
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