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Database: UniProt
Entry: V7Q0Y0_9BACT
LinkDB: V7Q0Y0_9BACT
Original site: V7Q0Y0_9BACT 
ID   V7Q0Y0_9BACT            Unreviewed;       456 AA.
AC   V7Q0Y0;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   25-OCT-2017, entry version 31.
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   ECO:0000313|EMBL:ETB64093.1};
GN   ORFNames=O210_OD1C00001G0576 {ECO:0000313|EMBL:ETB64093.1};
OS   Parcubacteria bacterium RAAC4_OD1_1.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1394712 {ECO:0000313|EMBL:ETB64093.1, ECO:0000313|Proteomes:UP000018547};
RN   [1] {ECO:0000313|EMBL:ETB64093.1, ECO:0000313|Proteomes:UP000018547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Kantor R.S., Wrighton K.C., Handley K.M., Sharon I., Hug L.A.,
RA   Castelle C.J., Thomas B.C., Banfield J.F.;
RT   "Small genomes and sparse metabolisms of sediment-associated bacteria
RT   from four candidate phyla.";
RL   Submitted (NOV-2013) to the EMBL/GenBank/DDBJ databases.
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: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:ETB64093.1}.
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DR   EMBL; AWSN01000001; ETB64093.1; -; Genomic_DNA.
DR   EnsemblBacteria; ETB64093; ETB64093; O210_OD1C00001G0576.
DR   PATRIC; fig|1394712.3.peg.542; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000018547; 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; 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: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.
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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000018547};
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:UP000018547}.
FT   DOMAIN      155    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      365    434       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     163    170       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   456 AA;  53020 MW;  41CA65EF4B0A7762 CRC64;
     MDTDIKKLWE DCLSEIELSI SKANFTTWFK NTHIVKEDLG TIIVGVPNEF VRDWLNNKFH
     KLILKTLIGR NESIRGVEYV IAKQEIKNID INNKNRSINI QNTNLLNKEL PLNDLYINKE
     DNLNPKYTFN SFIVGPFNEL AYAVAQAIIE NPGKNYNPFF VYGGTGLGKT HMIQSIGNTI
     KIKHPEKKIY YVSLEKFAMD YINSIQNKNP NSFKEKYRKY DVIIMDDIQF ISGKDKTQEE
     LFHLFNTLYE NNKQIIFSSD KHPNFIQGLE ERLQSRFASG MTVQITEPDY ESRIAIIKAK
     FENTNLVVEE DIISYLAEVL DGNIRELEGS LNTVVCQSQL KNKSLTLNEA KILIKNNIKP
     KKTVAIKDIV KIISEYYQLE EETIYDKTRR KEIVKARQVI MYILREDFNI SYPLIGQKLG
     DRDHTTVIHS HLKIKDDLKT DPSLLQEIEK IRILLK
//
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