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Database: UniProt
Entry: A0A0M9DSI1_9BACT
LinkDB: A0A0M9DSI1_9BACT
Original site: A0A0M9DSI1_9BACT 
ID   A0A0M9DSI1_9BACT        Unreviewed;       480 AA.
AC   A0A0M9DSI1;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-SEP-2017, entry version 15.
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=AD998_09465 {ECO:0000313|EMBL:KOY86340.1};
OS   bacterium 336/3.
OC   Bacteria.
OX   NCBI_TaxID=1664068 {ECO:0000313|EMBL:KOY86340.1, ECO:0000313|Proteomes:UP000037950};
RN   [1] {ECO:0000313|EMBL:KOY86340.1, ECO:0000313|Proteomes:UP000037950}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=336/3 {ECO:0000313|EMBL:KOY86340.1,
RC   ECO:0000313|Proteomes:UP000037950};
RA   Isojarvi J., Battchikova N., Aro E.-M.;
RT   "Draft genome sequence of symbiotic bacteroides-like organism.";
RL   Submitted (JUL-2015) 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: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:KOY86340.1}.
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DR   EMBL; LJIE01000001; KOY86340.1; -; Genomic_DNA.
DR   RefSeq; WP_054039215.1; NZ_LJIE01000001.1.
DR   EnsemblBacteria; KOY86340; KOY86340; AD998_09465.
DR   PATRIC; fig|1664068.3.peg.1919; -.
DR   Proteomes; UP000037950; 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: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:UP000037950};
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:UP000037950}.
FT   DOMAIN      170    300       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      387    456       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     178    185       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   480 AA;  55430 MW;  59E4FC8B755D21E1 CRC64;
     MIKDHRVVWE NCLRVIQQYL PEHTFKTWFG PVVPVSLHNN ILTIQVPSPF YYEWIEENYV
     DILRKAIDQE LGAEGKLEYS LVVDKGNAES LPKTMTVPNN KIELDIKSKE EKPNHDLQKR
     KQQIMKEHDA FFRDIQFNEN YTFDNFVEGD CNRLARSAGF AVAKKPGVTA FNPLMLYGGV
     GLGKTHLVQA IANHVRFNSP EKIVVYISSE KFVNQFIEEL KSNNLQKLTN FYLKIDVLII
     DDVQFLSGKE RTQEMFFHIF NHLHQHGKQI IMTSDRPPKE LQGLEDRLLS RFKWGLTADV
     QQPDFETRVA IIHRKLQNEG ISISYDVIDY LAHSIDSNIR ELEGVIVSLM ARSNLDRREI
     DVQLAKETVR HIVKKVDDRR PDDVEVGIDS IQRTVCQYFG VTEEELKGKA RTKALALARQ
     MAMYLCKEYT EFSLKAIGFH FGGRDHSTVI HAIQTISDLR EVDSSVRNDV AALMKILNKR
//
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