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Database: UniProt
Entry: A0A0F9Y084_9BACT
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ID   A0A0F9Y084_9BACT        Unreviewed;       498 AA.
AC   A0A0F9Y084;
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=SZ59_C0001G0036 {ECO:0000313|EMBL:KKP24718.1};
OS   candidate division TM6 bacterium GW2011_GWF2_28_16.
OC   Bacteria; Candidatus Dependentiae.
OX   NCBI_TaxID=1619077 {ECO:0000313|EMBL:KKP24718.1, ECO:0000313|Proteomes:UP000033842};
RN   [1] {ECO:0000313|EMBL:KKP24718.1, ECO:0000313|Proteomes:UP000033842}
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:KKP24718.1}.
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DR   EMBL; LBNX01000001; KKP24718.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKP24718; KKP24718; SZ59_C0001G0036.
DR   PATRIC; fig|1619077.4.peg.36; -.
DR   Proteomes; UP000033842; 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:UP000033842};
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:UP000033842}.
FT   DOMAIN      193    321       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      405    474       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     201    208       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   498 AA;  57321 MW;  A4A939A5E0F93FB2 CRC64;
     MDQIWQSFLK IIKEDVGIQT VETWFKAVSL EKWDKEKEIV FLNVPNQFVK NWLKEHYFII
     IQKTLKSLLD SENLNIEFLS PDPSLARTRN IIPASMIHTY TKTNNNTPEN SSNAGNTNNT
     STYTKPNIIY KDKQEDIPEN LNTNTQQLPA KTEFSFKKSN LNPNYNFDSF IIGPNNSLAH
     AAGYAICQNL GRVYNPLFIY GGTGLGKTHL LHAIGNEVKN RDNSKTIVYQ TIDKFTNEFI
     AAIRLDKIML FRQKYQKIDL LLLDDIQFLS NKEQTQEMFF HIFNLLYEEK KQIILSSDTF
     PKEIKGLQAR LKSRLEWGLV VDIQIPDLET KIAILEKKAE QNSINLTPEV SSFIASRITS
     NVRELEGALI RVNAFSTLTN KPLSLDLAKK VLLHLDDSTK KEGIMLEKIL RTITHHYSIS
     VNDLKSKKRH KDVALIRQIT FFLMKKLSYC SLKTIGESIG NRDHSTVLHA ITRVEENIKN
     DHDFAKKINN IEQKILMS
//
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