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Database: UniProt
Entry: F6EQR8_HOYSD
LinkDB: F6EQR8_HOYSD
Original site: F6EQR8_HOYSD 
ID   F6EQR8_HOYSD            Unreviewed;       568 AA.
AC   F6EQR8;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   05-JUL-2017, entry version 42.
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   ECO:0000313|EMBL:AEF38461.1};
GN   OrderedLocusNames=AS9A_0001 {ECO:0000313|EMBL:AEF38461.1};
OS   Hoyosella subflava (strain DSM 45089 / JCM 17490 / NBRC 109087 /
OS   DQS3-9A1) (Amycolicicoccus subflavus).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Hoyosella.
OX   NCBI_TaxID=443218 {ECO:0000313|EMBL:AEF38461.1, ECO:0000313|Proteomes:UP000009235};
RN   [1] {ECO:0000313|EMBL:AEF38461.1, ECO:0000313|Proteomes:UP000009235}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45089 / DQS3-9A1 {ECO:0000313|Proteomes:UP000009235};
RX   PubMed=21725023; DOI=10.1128/JB.05388-11;
RA   Cai M., Chen W.M., Nie Y., Chi C.Q., Wang Y.N., Tang Y.Q., Li G.Y.,
RA   Wu X.L.;
RT   "Complete genome sequence of Amycolicicoccus subflavus DQS3-9A1T, an
RT   actinomycete isolated from crude oil-polluted soil.";
RL   J. Bacteriol. 193:4538-4539(2011).
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}.
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DR   EMBL; CP002786; AEF38461.1; -; Genomic_DNA.
DR   STRING; 443218.AS9A_0001; -.
DR   EnsemblBacteria; AEF38461; AEF38461; AS9A_0001.
DR   KEGG; asd:AS9A_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; ATHIERN; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009235; Chromosome.
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:UP000009235};
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:UP000009235}.
FT   DOMAIN      261    389       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      473    541       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     269    276       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   568 AA;  63074 MW;  AA6FAA7DF6C6D25D CRC64;
     MDSWLRSVAE QVRFSRSSAH AVAVEMAGER TTTNVCGHQL EQRRVYTVEN DPRALADVWM
     KVVEELASGA SSEGPARMLS RKDRALLPLV KPLDISNGFA LLAAPTAFAK KAIESSLRDP
     ITESLSRHLG EPVELAVRIA ASSDVVPLGT ESTATAAQSS SLHDTSESDH SSYDVLVGNG
     DGPLGDDAPD TFGADPFESD TIDNASAGWP NYFTQTPRPP RAVSAKSSLN PKYTFDTFVI
     GASNRFAHAA AVAIAEAPAR AYNPLFVWGE SGLGKTHLLH ATGHYAQRLF PGMRVKYVST
     EEFTNDFINS LRDDRRVAFK RRYREIDLLL IDDIQFIENK EGIQEEFFHT FNTLHNANKQ
     ILISSDRPPK QLATLEERLR TRFEWGLITD VQPPELETRI AILSKKAQMD RLDVPDDVLA
     FIASRVERNI RELEGALIRV TAFASLNRQA IDLRLAEVVL RDLAPDSRTL EITAATIMST
     VAEYFGISVD ELCGPGRTRA VAQARQIAMY LCRELTDLSL PKIGQAFGRD HTTVMHADRK
     VRADMANSRR VYEQVQELTA RIRQRSKI
//
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