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Database: UniProt
Entry: A0A0G1PM02_9BACT
LinkDB: A0A0G1PM02_9BACT
Original site: A0A0G1PM02_9BACT 
ID   A0A0G1PM02_9BACT        Unreviewed;       485 AA.
AC   A0A0G1PM02;
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};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=UX00_C0012G0015 {ECO:0000313|EMBL:KKT97354.1};
OS   Microgenomates group bacterium GW2011_GWB1_45_17.
OC   Bacteria.
OX   NCBI_TaxID=1618506 {ECO:0000313|EMBL:KKT97354.1, ECO:0000313|Proteomes:UP000034461};
RN   [1] {ECO:0000313|EMBL:KKT97354.1, ECO:0000313|Proteomes:UP000034461}
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:SAAS00731907}.
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:KKT97354.1}.
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DR   EMBL; LCKN01000012; KKT97354.1; -; Genomic_DNA.
DR   EnsemblBacteria; KKT97354; KKT97354; UX00_C0012G0015.
DR   PATRIC; fig|1618506.3.peg.919; -.
DR   Proteomes; UP000034461; 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; 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|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000034461};
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:UP000034461}.
FT   DOMAIN      177    305       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      389    458       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     185    192       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   485 AA;  54596 MW;  8A7ED7987B4D0243 CRC64;
     MTPQELWEKS RPPLEDALSK RMYTFWFSTT ELTEIREVGE DRAIGVISGS SVFHLSNVEN
     KYYAHIKEVF DKLTGKKFEL QFAIKRGVKK QKSIAGGTGK GSSKKNPQEE FPNLFSQENQ
     RIEGSQEKGK TFPTSFTFAL QKAGLREDYA FETLAVSSSN EMAHAAAVAV SQNPGTAYNP
     LFLYGGVGVG KTHLMQAIGN NILRKNPQTP IAYITGEQFT NEIVAAIQQK RTIDLKKKFR
     NYKVLLVDDV QFIAGKNTVQ EEFFHTFNAI TPAGGQIILT SDRPPHEIML LEDRLRSRFE
     AGLIVDIQQP SFELRTAILL IKAKKLELDL PMDVAQRIAS AIESTRRLEG ILIKLHSEHT
     LFKKPISIEL VEEILGKIEK VEFPKQDIKP AEVLKTVAAQ FHLTTNSLKG PSRVKNLVEA
     RHIAMYILRY DLGVTLDQIG LLFNGRDHSS IIHATEKIKA TIIENEELRT RVNAVKTSLS
     FRQES
//
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