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Database: UniProt
Entry: A0A0G1TCX5_9BACT
LinkDB: A0A0G1TCX5_9BACT
Original site: A0A0G1TCX5_9BACT 
ID   A0A0G1TCX5_9BACT        Unreviewed;       492 AA.
AC   A0A0G1TCX5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   05-JUL-2017, entry version 15.
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=UY05_C0025G0005 {ECO:0000313|EMBL:KKU79624.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWA2_47_7.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619058 {ECO:0000313|EMBL:KKU79624.1, ECO:0000313|Proteomes:UP000034737};
RN   [1] {ECO:0000313|EMBL:KKU79624.1, ECO:0000313|Proteomes:UP000034737}
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:KKU79624.1}.
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DR   EMBL; LCON01000025; KKU79624.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU79624; KKU79624; UY05_C0025G0005.
DR   PATRIC; fig|1619058.3.peg.324; -.
DR   Proteomes; UP000034737; 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:UP000034737};
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:UP000034737}.
FT   DOMAIN      172    304       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      400    469       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     180    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   492 AA;  55873 MW;  7E1AA2D89A871D0A CRC64;
     MTNPCLLGEG DYNKIPMDTK ELWRQILLRI YPTLRHDQFI TWFADTTVLR VDGHVMVVGV
     PSQFAYSWIA KHYTANILEA GKTLNPAITE VSIVVDPSLT NADDTKKVSL ESVIPETKKV
     RKLPRKQEVK IDDDTVSYML NPNYQLHNFI VGKHNRLVHA ACLAVGSNPG AQWNPLFIYG
     GVGLGKTHLC QATGREILKN HPDKIVVYLT AERFLNEVVD AIKKYNAQDF KARYRNVDCL
     IIDDIQLLAD KDRTQEEFFH LFNELYNANK QIIISSDRPP KELAGIETRL QSRFEMGMVA
     EVHFPDYEKR LAILQNKCAE QQLFVAPEVL DFIAYNVHHS VRELEGVLMQ ASAQMRLENI
     TPTVKSVGGI LRKLDRNGDV AATAQAQGNS SPDNKSSIRS ADDVINLVAD YYRIPSSELR
     GPSRKREIML PRQLCMYLIY EVLGHSYDTI GDYFSGRNHT TVLHSYNKVK SRIGKDSKML
     QDIHSIKKEM GL
//
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