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Database: UniProt
Entry: G6XI45_9PROT
LinkDB: G6XI45_9PROT
Original site: G6XI45_9PROT 
ID   G6XI45_9PROT            Unreviewed;       472 AA.
AC   G6XI45;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-SEP-2017, entry version 38.
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=GMO_12550 {ECO:0000313|EMBL:EHH68484.1};
OS   Gluconobacter morbifer G707.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Gluconobacter.
OX   NCBI_TaxID=1088869 {ECO:0000313|EMBL:EHH68484.1, ECO:0000313|Proteomes:UP000004949};
RN   [1] {ECO:0000313|EMBL:EHH68484.1, ECO:0000313|Proteomes:UP000004949}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G707 {ECO:0000313|EMBL:EHH68484.1,
RC   ECO:0000313|Proteomes:UP000004949};
RA   Lee W.-J., Kim E.-K.;
RT   "Genome sequence of Gluconobacter morbifer G707, isolated from
RT   Drosophila gut.";
RL   Submitted (OCT-2011) 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:EHH68484.1}.
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DR   EMBL; AGQV01000002; EHH68484.1; -; Genomic_DNA.
DR   EnsemblBacteria; EHH68484; EHH68484; GMO_12550.
DR   PATRIC; fig|1088869.3.peg.1258; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000004949; 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:UP000004949};
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:UP000004949}.
FT   DOMAIN      170    300       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      380    449       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     178    185       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   472 AA;  53248 MW;  13D83F619481F748 CRC64;
     MEHAQYLDAS ASAPGTANPL EAAWHRVREK LKSEVGEVEY RTWLRQIVLG PLEEDELILY
     LPTRFLRDWV RSQYGDRLQT LWRNERDDVQ AIELQVKRGL PEIPADEGSE KEEPSSEPLP
     SASVSAPEIR SDLTVPLDPR FTFDTFVVGK PNEFAYACAR RVAEKPSSPG FNPLFLYGGV
     GLGKTHLMHA IGTELTKTGN VSVAYMSAEK FMYRFIAAIR SQSTMEFKEQ LRSVDVLMID
     DLQFLIGKDN TQEEFFHTFN ALVDAGRQII VSADKSPSDL SGLEDRLRTR LGCGMVADIH
     ATTFELRISI LEAKAKASGT HVPSKVLEYL AHKITTNVRE LEGALNRLIA HADLVGRPVT
     LDTTQDVLKD MLKAHDRRVT IEEIQRKVAE HWNIRLTDMS SARRARAVAR PRQVAMFLAK
     QLTSRSLPEI GRKFGNRDHT TVMHAVNRVA ELMDQDVSFA EDVELLRRML EG
//
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