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Database: UniProt
Entry: M5AFI7_9ACTN
LinkDB: M5AFI7_9ACTN
Original site: M5AFI7_9ACTN 
ID   M5AFI7_9ACTN            Unreviewed;       478 AA.
AC   M5AFI7;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, 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   ECO:0000313|EMBL:BAN00315.1};
GN   ORFNames=YM304_00010 {ECO:0000313|EMBL:BAN00315.1};
OS   Ilumatobacter coccineus YM16-304.
OC   Bacteria; Actinobacteria; Acidimicrobiia; Acidimicrobiales;
OC   Acidimicrobiaceae; Ilumatobacter.
OX   NCBI_TaxID=1313172 {ECO:0000313|EMBL:BAN00315.1, ECO:0000313|Proteomes:UP000011863};
RN   [1] {ECO:0000313|EMBL:BAN00315.1, ECO:0000313|Proteomes:UP000011863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YM16-304 {ECO:0000313|EMBL:BAN00315.1};
RX   PubMed=23524358; DOI=10.1099/ijs.0.047316-0;
RA   Matsumoto A., Kasai H., Matsuo Y., Shizuri Y., Ichikawa N., Fujita N.,
RA   Omura S., Takahashi Y.;
RT   "Ilumatobacter nonamiense sp. nov. and Ilumatobacter coccineum sp.
RT   nov., isolated from seashore sand.";
RL   Int. J. Syst. Evol. Microbiol. 63:3404-3408(2013).
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; AP012057; BAN00315.1; -; Genomic_DNA.
DR   RefSeq; WP_015439563.1; NC_020520.1.
DR   EnsemblBacteria; BAN00315; BAN00315; YM304_00010.
DR   KEGG; aym:YM304_00010; -.
DR   PATRIC; fig|467094.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011863; Chromosome.
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:UP000011863};
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:UP000011863}.
FT   DOMAIN      174    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      386    455       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     182    189       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   478 AA;  53849 MW;  CE954F1D0D722897 CRC64;
     MPVTEADDVW TQVTLALRMQ LAESVWFSTF QDVQPISADN DTLRLLAPSG YVRDRILKRY
     LPLVTDALED AGEGHRTIEI DVKAGADHDE SVPDEHHAAP IDNAPADTAH QSDTANTPSN
     IHLDTGPAAL SERDLVLEDA GLSSDYSFET FVKGASNQFA LAAALRVAET PARSYNPLFI
     YGAAGLGKTH LLYAIGHYVH SNYQHHKVRY VSTETFMNEY VESIRQNTTN LLRQRYRDVD
     VLLIDDIQFI ANKEGLQEEF FHTFNALHGA NKQIVISSDR TPDNIPTLEE RLRSRFKWGL
     ITDIQPPDVE TRLAILRNKA DREDVDVPAA ALEFIAENIS TNIRELEGAL VRVMAFASLS
     RQPITIDLVQ SQLEDLLTLS QPKIRTDEEL LQEIADILRF DVEALKGKSR QRPLVTARQI
     AMYVFRDLTD LSYPAIARLF GGRDHTTVIH ANDKIQRLMK ERKEIYDQVT ALILKLKA
//
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