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Database: UniProt
Entry: A0A0G0CEH4_9BACT
LinkDB: A0A0G0CEH4_9BACT
Original site: A0A0G0CEH4_9BACT 
ID   A0A0G0CEH4_9BACT        Unreviewed;       495 AA.
AC   A0A0G0CEH4;
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};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=UR78_C0011G0012 {ECO:0000313|EMBL:KKP79598.1};
OS   Candidatus Moranbacteria bacterium GW2011_GWF2_35_39.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1618721 {ECO:0000313|EMBL:KKP79598.1, ECO:0000313|Proteomes:UP000034839};
RN   [1] {ECO:0000313|EMBL:KKP79598.1, ECO:0000313|Proteomes:UP000034839}
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: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:KKP79598.1}.
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DR   EMBL; LBQM01000011; KKP79598.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP79598; KKP79598; UR78_C0011G0012.
DR   PATRIC; fig|1618721.3.peg.565; -.
DR   Proteomes; UP000034839; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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; 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.
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:UP000034839};
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034839};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM     15     36       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      189    321       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      401    470       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     197    204       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   495 AA;  56609 MW;  2DB7FF8645B6E008 CRC64;
     MNLHFFCQNY FHPHFINNVI HFSLRLFFGV VLYFFYMTNE ELWKTALGEI ELSISKANFI
     TWFKNTSIFS IKDGHVVISV PNGFAKEWLE NKYDLYILRA LKNIQGDIKS VSCLISTGPT
     TFFPQKNSEP TVDAIQAPKK ASFPTEKKLF ISRENNLNPK YTFDNFVVGG SNELAKAACY
     AVSQNLGNVY NPLFIYGGVG LGKTHLIQSI GNEVLKSNPQ LQIKYISSER FTSELIDSIK
     NQKIKEFKEY YQKIDLLIID DIQFISGKEK TQEEFFHIFN YLYQLNKQII LSSDRAPKAI
     QILEERLRSR FEGGMIADVS KPDLETRLAI LKKKATQNNI EITPDALDYI ASNIKNNIRE
     LEGALNRVLV SAQLTKKVVD LAYTKQILSD IISSGKKRGV SYKHILKVVS DFYEVSLDDL
     IAKNRKQEVV KPRQVAMFLM RSELAFSYPG IGDKLGGRDH TTAIHACDKI LQALKEDEKL
     NEELVHLKDL LYLLP
//
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