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Database: UniProt
Entry: F7XUH8_MIDMI
LinkDB: F7XUH8_MIDMI
Original site: F7XUH8_MIDMI 
ID   F7XUH8_MIDMI            Unreviewed;       476 AA.
AC   F7XUH8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   05-JUL-2017, entry version 44.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:AEI88327.1};
GN   OrderedLocusNames=midi_00001 {ECO:0000313|EMBL:AEI88327.1};
OS   Midichloria mitochondrii (strain IricVA).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Candidatus Midichloriaceae; Candidatus Midichloria.
OX   NCBI_TaxID=696127 {ECO:0000313|EMBL:AEI88327.1, ECO:0000313|Proteomes:UP000006639};
RN   [1] {ECO:0000313|EMBL:AEI88327.1, ECO:0000313|Proteomes:UP000006639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IricVA {ECO:0000313|EMBL:AEI88327.1,
RC   ECO:0000313|Proteomes:UP000006639};
RX   PubMed=21690562; DOI=10.1093/molbev/msr159;
RA   Sassera D., Lo N., Epis S., D'Auria G., Montagna M., Comandatore F.,
RA   Horner D., Pereto J., Luciano A.M., Franciosi F., Ferri E., Crotti E.,
RA   Bazzocchi C., Daffonchio D., Sacchi L., Moya A., Latorre A., Bandi C.;
RT   "Phylogenomic evidence for the presence of a flagellum and cbb3
RT   oxidase in the free-living mitochondrial ancestor.";
RL   Mol. Biol. Evol. 28:3285-3296(2011).
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}.
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; CP002130; AEI88327.1; -; Genomic_DNA.
DR   STRING; 696127.midi_00001; -.
DR   EnsemblBacteria; AEI88327; AEI88327; midi_00001.
DR   KEGG; mmn:midi_00001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; VENWVKD; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006639; 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; 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.
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:UP000006639};
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:UP000006639}.
FT   DOMAIN      169    313       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      379    448       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     177    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   476 AA;  54094 MW;  09B845763E1A64E7 CRC64;
     MDLNHLPHNL VLDKDGVNEG MFVYNALLEK IKEEYGNTVF TNWFAHMAFK SLSDQTLTIV
     APSKFVREWV ILNYFTKIYK ILELFNGLVK RIDIIVETSP SSIELPVLSN SQVNKVEAVT
     EIDKSDFSFS FDTRFSFENF AVGFSNKMAF SAAQNMAGFN HNWHSSAINY NILFIHGAVG
     MGKTHLLYAI ANSISKAYPE KSICYLSAEK FMHRYMMAVR KNELINFKEN LRSLDILLFD
     DLQFICDKSS TQKEFANTIN ALIESNKKIV IACDRSPYNL DLDPRTKSRV ASGVIAEIQA
     ADFNLRLNIL KQKSNLMQIT IEDEILSYLA TSISSNIREL EGSLNKLVTY CSLNEMPITL
     ETCKNTLKDC IKAHEQDVSV AKIIQAVADL SGVTKVEILS KSRLAKLVYL RQMVAYLAKE
     ITKSSLQEIG KQLGGKDHAT IIYYIRQFEQ KIERRPAIKD ELDNIKKLVK GHIMAR
//
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