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Database: UniProt
Entry: M1LT72_9PROT
LinkDB: M1LT72_9PROT
Original site: M1LT72_9PROT 
ID   M1LT72_9PROT            Unreviewed;       473 AA.
AC   M1LT72;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   25-OCT-2017, entry version 39.
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=ST1E_0224 {ECO:0000313|EMBL:AGF48727.1};
OS   Candidatus Kinetoplastibacterium galatii TCC219.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Kinetoplastibacterium.
OX   NCBI_TaxID=1208921 {ECO:0000313|EMBL:AGF48727.1, ECO:0000313|Proteomes:UP000011658};
RN   [1] {ECO:0000313|EMBL:AGF48727.1, ECO:0000313|Proteomes:UP000011658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC219 {ECO:0000313|EMBL:AGF48727.1};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J.,
RA   Matveyev A.V., Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of
RT   strigomonas and angomonas.";
RL   Genome Biol. Evol. 5:338-350(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:SAAS00911680}.
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; CP003806; AGF48727.1; -; Genomic_DNA.
DR   RefSeq; WP_015389212.1; NC_020284.1.
DR   EnsemblBacteria; AGF48727; AGF48727; ST1E_0224.
DR   KEGG; kga:ST1E_0224; -.
DR   PATRIC; fig|1208921.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011658; 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:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011658};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011658}.
FT   DOMAIN      169    303       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      381    450       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     177    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  53852 MW;  2084131A5950F3F9 CRC64;
     MEDFWLSFIS NLEKELPHQQ ISAWIKPLIP ISFDESKSIL RILAPNRFKL DLVKKKFASQ
     IEILASDWFK KPVNVIFELP VVNNERIVHK KNDILTPVIG NYIYNGKTDD SIGLINQKVD
     VSLSNEATNR AYERSRLNTV LTFDSFVTGK ANQLARAASL QVSENPGVSY NPLFLYGGVG
     LGKTHLIHAV GNAMLCARND VKVRYVHADQ YVSDVVKAYQ RKAFDEFKKY YHSLDLLLID
     DIQFFSGKNR TQEEFFYAFE AMVAQHKQII ITSDTYPKEL SGIDSRLISR FDSGLTVAIE
     PPELEMRVAI LLRKAKSENL PMPEEVAFFI AKHLRSNVRE LEGALRKVLA YVRFHGRNVL
     TVDVCKEALK DLLSVSNGQI TVENIQKTVA DYYKIKVADM YSKRRPANIA LPRQIAMYLS
     KELTQKSLPE IGDLFGGRDH TTVLHAVRKI SDARIKQTEL NHNLHVLEQT LKG
//
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