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Database: UniProt
Entry: D6SNZ9_9DELT
LinkDB: D6SNZ9_9DELT
Original site: D6SNZ9_9DELT 
ID   D6SNZ9_9DELT            Unreviewed;       449 AA.
AC   D6SNZ9;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   27-SEP-2017, entry version 42.
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=Dthio_PD1834 {ECO:0000313|EMBL:EFI34475.1};
OS   Desulfonatronospira thiodismutans ASO3-1.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfohalobiaceae; Desulfonatronospira.
OX   NCBI_TaxID=555779 {ECO:0000313|EMBL:EFI34475.1, ECO:0000313|Proteomes:UP000005496};
RN   [1] {ECO:0000313|EMBL:EFI34475.1, ECO:0000313|Proteomes:UP000005496}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ASO3-1 {ECO:0000313|EMBL:EFI34475.1,
RC   ECO:0000313|Proteomes:UP000005496};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Land M.L.,
RA   Hauser L., Kyrpides N., Mikhailova N., Muyzer G., Woyke T.;
RT   "The draft genome of Desulfonatronospira thiodismutans ASO3-1.";
RL   Submitted (MAY-2010) 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:EFI34475.1}.
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DR   EMBL; ACJN02000002; EFI34475.1; -; Genomic_DNA.
DR   RefSeq; WP_008869797.1; NZ_ACJN02000002.1.
DR   STRING; 555779.Dthio_PD1834; -.
DR   EnsemblBacteria; EFI34475; EFI34475; Dthio_PD1834.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000005496; 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:UP000005496};
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:UP000005496}.
FT   DOMAIN      144    281       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     152    159       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  50873 MW;  869B5B654015CE04 CRC64;
     MTDAWERIQI ILEKSLKSGI FQLWIKPLQG SFDPDAKILR LQAPNEFVAS WVRERLQSMI
     LEAGQDVLGV TPELEISAFR ADEAASPLGS PEKAGASETR MHLPIQSNIQ VVSRFRYSFQ
     DFVVGPSNEL AFVASRSFCR EQVSSDQLFL CSSTGLGKTH LVQSMGNNLA GSSNKEALRV
     AYLTAEEFAC QLIQAIKSKQ VERFKARYRD QIDILMLEDI HFFQGKEKIQ GEFLSTINSL
     QGQGKKVVLS SSFLPKELND LDSNLVSRLC RGFMAVIDKP DLGTRQEILR QKASSLQISL
     PQEVSHLLAE RIQTDIRQLE SCLSNLVFKA RMLKERITLE MALEVLKNYD LKEQNLDLEE
     IIRSVCRVFD LPREKVCSKS RKKQHVLARN LAFYLARKYT GHSLKDIGRR FNRRHSTVLK
     GVANVEKEVN TDTPLGRQLK DAASRVMPN
//
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