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Database: UniProt
Entry: A0A101HZT9_9BACT
LinkDB: A0A101HZT9_9BACT
Original site: A0A101HZT9_9BACT 
ID   A0A101HZT9_9BACT        Unreviewed;       354 AA.
AC   A0A101HZT9;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   05-JUL-2017, entry version 11.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|RuleBase:RU000577};
DE   Flags: Fragment;
GN   ORFNames=XE01_0995 {ECO:0000313|EMBL:KUK86161.1};
OS   Synergistales bacterium 58_81.
OC   Bacteria; Synergistetes; Synergistia; Synergistales.
OX   NCBI_TaxID=1635274 {ECO:0000313|EMBL:KUK86161.1, ECO:0000313|Proteomes:UP000054873};
RN   [1] {ECO:0000313|EMBL:KUK86161.1, ECO:0000313|Proteomes:UP000054873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=58_81 {ECO:0000313|EMBL:KUK86161.1};
RA   Hu P., Tom L., Singh A., Thomas B.C., Baker B.J., Piceno Y.M.,
RA   Andersen G.L., Banfield J.F.;
RT   "Genome-resolved metagenomic analysis reveals roles for candidate
RT   phyla and other microbial community members in biogeochemical
RT   transformations in oil reservoirs.";
RL   MBio 7:e01669-15(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|RuleBase:RU000577}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00731929}.
CC   -!- SIMILARITY: Belongs to the DnaA family.
CC       {ECO:0000256|RuleBase:RU004227, 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:KUK86161.1}.
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DR   EMBL; LGGV01000054; KUK86161.1; -; Genomic_DNA.
DR   PATRIC; fig|1635274.3.peg.554; -.
DR   Proteomes; UP000054873; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:InterPro.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:InterPro.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:InterPro.
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; 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   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|RuleBase:RU000577,
KW   ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000054873};
KW   Cytoplasm {ECO:0000256|SAAS:SAAS00731880};
KW   DNA replication {ECO:0000256|RuleBase:RU004227,
KW   ECO:0000256|SAAS:SAAS00731887};
KW   DNA-binding {ECO:0000256|RuleBase:RU000577,
KW   ECO:0000256|SAAS:SAAS00731910};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000577,
KW   ECO:0000256|SAAS:SAAS00731897};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054873}.
FT   DOMAIN       52    180       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      264    333       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NON_TER       1      1       {ECO:0000313|EMBL:KUK86161.1}.
SQ   SEQUENCE   354 AA;  40270 MW;  AAC791B5395D9F50 CRC64;
     EEIKRAERIS RESERPKNGL NPDYQFDSFV VGKSNRLAHA ASLAVAESPG VAYNPLFFWG
     GVGLGKTHLL HAIGNFVTKH NEGTKIAYIS SEKFINEFIL SIQNNKTHEF KQKYRSVDVL
     LIDDIHFLAN KESTQEEFFH TFNSLHDAKK QIVLTSDKPP KDIHNIEERL VSRFEWGLVT
     DIQPPDLETR IAILKKKAAL KNYFVPDDVI DFLAQNIPSN IRELEGSLNS VMFFADLNNE
     SVTVENASRW LKDLIRRSSR GQITIELIQQ VTAESFGIPV SSLSGNKRTS EIALARQVAM
     YLSRDMTGTT LQQIGYAFNR KDHTTVIHAC KKIEESLRKD SRIKSIVENL REKL
//
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