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Database: UniProt
Entry: L0EWG1_LIBCB
LinkDB: L0EWG1_LIBCB
Original site: L0EWG1_LIBCB 
ID   L0EWG1_LIBCB            Unreviewed;       501 AA.
AC   L0EWG1;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   05-JUL-2017, entry version 34.
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   OrderedLocusNames=B488_11930 {ECO:0000313|EMBL:AGA65185.1};
OS   Liberibacter crescens (strain BT-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Liberibacter.
OX   NCBI_TaxID=1215343 {ECO:0000313|EMBL:AGA65185.1, ECO:0000313|Proteomes:UP000010799};
RN   [1] {ECO:0000313|EMBL:AGA65185.1, ECO:0000313|Proteomes:UP000010799}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-1 {ECO:0000313|EMBL:AGA65185.1,
RC   ECO:0000313|Proteomes:UP000010799};
RX   PubMed=23408754;
RA   Leonard M.T., Fagen J.R., Davis-Richardson A.G., Davis M.J.,
RA   Triplett E.W.;
RT   "Complete genome sequence of Liberibacter crescens BT-1.";
RL   Stand. Genomic Sci. 7:271-283(2012).
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; CP003789; AGA65185.1; -; Genomic_DNA.
DR   RefSeq; WP_015273610.1; NC_019907.1.
DR   EnsemblBacteria; AGA65185; AGA65185; B488_11930.
DR   KEGG; lcc:B488_11930; -.
DR   PATRIC; fig|1215343.11.peg.1231; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000010799; 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:UP000010799};
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:UP000010799}.
FT   DOMAIN      194    321       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      409    478       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     202    209       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   501 AA;  57202 MW;  E06AB97360203B15 CRC64;
     MQLREISTYA QDNEVKIIKE TRPQDNVMET LDMRYSLLFE RVALRLKNHV GSDVYASWFQ
     RLKFHSILNN VIHLSVPTTF LKAWIKNRYL EIITKLFQEE DKTILKVDVV VRTATRFSSE
     KPSLPVSSQS YSPLKPISSN VITSTLNPKT VSPLFGSPLD TRFTFSSFIE GSSNRVALAA
     ARTIAEMGAK STVRFNPLFI HASVGLGKTH LLQAIANEAI ENKDGLRIVY LTAEYFMWRF
     ATAIRDNCAL NLKDSLRNID LLMIDDMQFL QGKLIQHEFC HLLNALLDSA KTVVVAADRP
     PSELESLDPR VRSRLQGGVS LELGSHDYDI RLAILKNRLK NSQIGDTSLN IPEEILVHVA
     RSITSSGREL DGAFNQLVFR HSFEPLLTID LVDEILTHLI KSSEPRRIRI EDIQRLVSRH
     YNVSRQDLLS SRRTRVVVKP RQIAMYLSKI MTTRSFPEIG RRFGDRDHTT VLHAVRKVET
     MLETDTKLLK EIELLKRLIA E
//
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