GenomeNet

Database: UniProt
Entry: A0A0G1R2G4_9BACT
LinkDB: A0A0G1R2G4_9BACT
Original site: A0A0G1R2G4_9BACT 
ID   A0A0G1R2G4_9BACT        Unreviewed;       461 AA.
AC   A0A0G1R2G4;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   25-OCT-2017, entry version 17.
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   ORFNames=UX72_C0021G0024 {ECO:0000313|EMBL:KKU51381.1};
OS   Parcubacteria group bacterium GW2011_GWA2_47_10.
OC   Bacteria; unclassified Parcubacteria group.
OX   NCBI_TaxID=1618839 {ECO:0000313|EMBL:KKU51381.1, ECO:0000313|Proteomes:UP000034777};
RN   [1] {ECO:0000313|EMBL:KKU51381.1, ECO:0000313|Proteomes:UP000034777}
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}.
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}.
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:KKU51381.1}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; LCNG01000021; KKU51381.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKU51381; KKU51381; UX72_C0021G0024.
DR   PATRIC; fig|1618839.3.peg.1068; -.
DR   Proteomes; UP000034777; Unassembled WGS sequence.
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; 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.
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:UP000034777};
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:UP000034777}.
FT   DOMAIN      157    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      368    437       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     165    172       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   461 AA;  52536 MW;  8D1FD289804E12FC CRC64;
     MELSDLWKTA LSEIELSVGR ASFVTWFKDT AIIDADNGRI MVSVPNGFAK EWLQNKYNKF
     ILRAIRNLNP EIKEVGFTIG KPQLAAVRTD RPIQIKKRLM DISEDSSLAS EFELKDMNIN
     PETNLNPKYT FDSFVVGSFN ELAHAAAQSV VKQSGHVYNP LFIYGGVGLG KTHLIQSIGN
     ELIKQNPKVK VKYVSSEKFM GEIVEALKNQ EMNQLKEKYR TCDLLIMDDI QFMAKTEKMQ
     EEFFHTFNAL YESNKQIVIS SDRPPAAIAT LEDRLKSRFE GGMIADIGEP DYETKLTILK
     LKAEKKGVSI QPEILEYVAQ TIKSNIRELE GALNRIILTS KMSNLPPSLE DVKKTLNQVI
     YAPRKFATPK KIIKAVADFY EISEKEIINR SRKKGVVKPR QVAMYLLRDE LKCSFPFIGE
     KLGRKDHTTA IHAYKKIVDE IKTNLNLEEE IKLIKEKVYT S
//
DBGET integrated database retrieval system