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Database: UniProt
Entry: A0A0S7X6L9_9BACT
LinkDB: A0A0S7X6L9_9BACT
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ID   A0A0S7X6L9_9BACT        Unreviewed;       447 AA.
AC   A0A0S7X6L9;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-SEP-2017, entry version 12.
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=AMJ49_00365 {ECO:0000313|EMBL:KPJ57564.1};
OS   Parcubacteria bacterium DG_74_2.
OC   Bacteria; Candidatus Parcubacteria.
OX   NCBI_TaxID=1703766 {ECO:0000313|EMBL:KPJ57564.1, ECO:0000313|Proteomes:UP000051668};
RN   [1] {ECO:0000313|EMBL:KPJ57564.1, ECO:0000313|Proteomes:UP000051668}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG_74_2 {ECO:0000313|EMBL:KPJ57564.1};
RX   PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT   "Genomic resolution of linkages in carbon, nitrogen, and sulfur
RT   cycling among widespread estuary sediment bacteria.";
RL   Microbiome 3:14-14(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:KPJ57564.1}.
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DR   EMBL; LJNF01000001; KPJ57564.1; -; Genomic_DNA.
DR   PATRIC; fig|1703766.3.peg.744; -.
DR   Proteomes; UP000051668; 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:UP000051668};
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:UP000051668}.
FT   DOMAIN      144    289       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      355    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   447 AA;  51749 MW;  3910EE8C37CF939B CRC64;
     MEKEELWQSV LAQIQLNISP ANFTTWFKNT NVISLKEGEV LISAPSSFVK EWLEQKYNKL
     ILKILRSLDQ KIKEVKYIVG KNKPKSLKKL PSFLEIGQLE FQEFKANRET NLNPRYTFEN
     FIVGSFNELA YAAAKAVCEN PGFVYNPLFV YGGVGLGKTH LLEAVGNEIV KKFPQRKVKY
     IPSENLVSQI VDSIRKREID NFKLKVQEVD VLVVDDVQFL SGKEKTQEEF FHIFNNLYAK
     NKQIVLSSDK PPRALQYLTE RLKSRFEGGM IADISQPDLE TRIAILKEKS SERKFEFPES
     ILNYIASNIT QNIRRLEGAL NRMATYQKLN GKVPDLEIVK ILLKDIIISP NKVITPKKII
     QATAEFYDLK EKDLLSKSRR KEIVKPRQIA MYLLRKELKG SFPFIGRKLK KDHTTVIYAF
     EKISKTIEKN EDLNQEINMI KERISSF
//
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