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Database: UniProt
Entry: A0A0G0MZT5_9BACT
LinkDB: A0A0G0MZT5_9BACT
Original site: A0A0G0MZT5_9BACT 
ID   A0A0G0MZT5_9BACT        Unreviewed;       473 AA.
AC   A0A0G0MZT5;
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, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377,
GN   ECO:0000313|EMBL:KKR08673.1};
GN   ORFNames=UT36_C0005G0044 {ECO:0000313|EMBL:KKR08673.1};
OS   Candidatus Peregrinibacteria bacterium GW2011_GWF2_39_17.
OC   Bacteria; Candidatus Peregrinibacteria.
OX   NCBI_TaxID=1619067 {ECO:0000313|EMBL:KKR08673.1, ECO:0000313|Proteomes:UP000034818};
RN   [1] {ECO:0000313|EMBL:KKR08673.1, ECO:0000313|Proteomes:UP000034818}
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: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:KKR08673.1}.
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DR   EMBL; LBWM01000005; KKR08673.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKR08673; KKR08673; UT36_C0005G0044.
DR   PATRIC; fig|1619067.4.peg.601; -.
DR   Proteomes; UP000034818; 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:UP000034818};
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:UP000034818}.
FT   DOMAIN      159    293       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    450       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     167    174       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   473 AA;  54358 MW;  0B27194CDB918401 CRC64;
     MVDVARDFWV QVLGALEPQL KRSDFLTWFQ HSALLERQAS KVIIGFPTVL TRDWVVNKYH
     AKILEALKVC DANIETVIYE VDGTLSNPEH NLSIDIKILS PTFKKVRKIR NKDELTVNVD
     GVRSKALNPK YTLDTYVIGQ ENRLAHAACM AVGKRPGTAY NPLFVYGDVG LGKTHLLQGT
     GNMILRNNSN AVVAYMTSEQ FTSEIVEAIR RHGANSFKDR YRNVDCLIID DIQFLAHKER
     TQEEFFHTFN SLYDNNRQVI ISADRPPKEL SDIQDRLISR FEMGMIVDVQ FPDYETRLAI
     LHCKCREHQV LLPNEVLEFI AFNVHHSIRE LEGILLRAIA QYELEQSAPT VRSVATIMKK
     LNRGGEFAVL EEGREHRSLA KTAEDIIEIV SDYYKLTRSD LTGPLRKKEV LLPRQICMYL
     IRKELDASYE QIGEEFGRNH TTVMHAFEKI IRLMRKDGKL IRDINALKQE MGL
//
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