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Database: UniProt
Entry: A0A0G1KZF5_9BACT
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ID   A0A0G1KZF5_9BACT        Unreviewed;       468 AA.
AC   A0A0G1KZF5;
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, ECO:0000256|SAAS:SAAS00724181};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=VE96_C0001G0014 {ECO:0000313|EMBL:KKT53259.1};
OS   candidate division Kazan bacterium GW2011_GWA1_44_22.
OC   Bacteria; candidate division Kazan-3B-28.
OX   NCBI_TaxID=1620410 {ECO:0000313|EMBL:KKT53259.1, ECO:0000313|Proteomes:UP000034752};
RN   [1] {ECO:0000313|EMBL:KKT53259.1, ECO:0000313|Proteomes:UP000034752}
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:KKT53259.1}.
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DR   EMBL; LCIJ01000001; KKT53259.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT53259; KKT53259; VE96_C0001G0014.
DR   PATRIC; fig|1620410.3.peg.15; -.
DR   Proteomes; UP000034752; 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:UP000034752};
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:UP000034752}.
FT   DOMAIN      157    288       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      369    438       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     165    172       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   468 AA;  53312 MW;  54E8F2DE034EA617 CRC64;
     MVDNKRLWQS VLGEAEIALS PANFSTWFKN TEIINASETV VFIRVPNIFT KEWFEKKYEK
     EIITKCLLRN LPHLGKIEYV IGVKPQRETI FNEPTTLKST ERLLERPPIA TLIKTRGTGE
     TIERLNPRYT FETFVIGESN HLAQAASEAV AKAPGTTYNP LFIYGGVGLG KTHLLQAIGN
     AILTNYPKKK VVYITSERFT NELVDSILKK TTREFKEKYR RVDCLLIDDV QFLEGKDATQ
     EEFFHTFNAL YESSKQIVLT SDRPPKAIAA LEARLRSRFE WGMMADITAP NYETRLAILR
     SKSANLKFPL ADNILELIAQ KIQNNIRELE GALTRTVAFG QLNNTVPTIE EAEGLLGGIL
     ISPGKKILRA HDIIRTVSKY YDLKKEDLLG KQRNKEIVVP RQILIYLLRE ELDLPYTAIA
     REIGGKDHTT IIHNYNKIKN LVLENTDLEN EILSIKEKLY SVDTNGKS
//
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