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Database: UniProt
Entry: A0A0G0XMN3_9BACT
LinkDB: A0A0G0XMN3_9BACT
Original site: A0A0G0XMN3_9BACT 
ID   A0A0G0XMN3_9BACT        Unreviewed;       454 AA.
AC   A0A0G0XMN3;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 16.
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=UU87_C0003G0055 {ECO:0000313|EMBL:KKS26135.1};
OS   Parcubacteria group bacterium GW2011_GWA2_42_11.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618819 {ECO:0000313|EMBL:KKS26135.1, ECO:0000313|Proteomes:UP000033821};
RN   [1] {ECO:0000313|EMBL:KKS26135.1, ECO:0000313|Proteomes:UP000033821}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a
RT   large radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKS26135.1}.
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DR   EMBL; LCCH01000003; KKS26135.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKS26135; KKS26135; UU87_C0003G0055.
DR   PATRIC; fig|1618819.3.peg.308; -.
DR   Proteomes; UP000033821; Unassembled WGS sequence.
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:UP000033821};
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:UP000033821}.
FT   DOMAIN      150    282       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      361    430       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     158    165       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   454 AA;  52237 MW;  79E26C119FEE58A1 CRC64;
     MNEQELWQAA LGDIELNISR ANFITWFRST SIIKNNDGII TVAVPNGFSK EWLQNKYNKL
     ILRSLRNLSP EIRDINFIIT QNKTDETPKK HRAPITRKNE SVANQPFQEF IVDKETNLNP
     KYKFDNFIVG GFNELAQAAT MAVINKPGEA YNPLFIYGGV GLGKTHLLQA AGNEIIQKHK
     NKKVKYISSD KFTSELVDSL HNGRMEEFKD AYRKIDVLII DDIQFLSGKE KTQEEFFHTF
     NALYQKNKQI ILSSDRPPKS IATLEERLRS RFEGGMIADI SFPDFETRLA ILKIKAQEKN
     LSLNDEALNY IATHIQKNIR ELEGALNSLN ASLKLKTTAP DLSQVQKALT HIIANPKRIT
     NFRGVLQAVA EFYDIELGEL TNRSRKKEVV YPRQIAMFLM REDLKNSFPF IGEKLGGRDH
     TTVMYAHEKM LRELENNESL QQEINLIRER IYNN
//
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