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Database: UniProt
Entry: K4KY61_9FIRM
LinkDB: K4KY61_9FIRM
Original site: K4KY61_9FIRM 
ID   K4KY61_9FIRM            Unreviewed;       445 AA.
AC   K4KY61;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   05-JUL-2017, entry version 36.
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   ECO:0000313|EMBL:AFV04007.1};
GN   ORFNames=DCF50_p1 {ECO:0000313|EMBL:AFV04007.1};
OS   Dehalobacter sp. CF.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Dehalobacter.
OX   NCBI_TaxID=1131462 {ECO:0000313|EMBL:AFV04007.1, ECO:0000313|Proteomes:UP000000482};
RN   [1] {ECO:0000313|EMBL:AFV04007.1, ECO:0000313|Proteomes:UP000000482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CF {ECO:0000313|EMBL:AFV04007.1};
RX   PubMed=23284863; DOI=10.1371/journal.pone.0052038;
RA   Tang S., Gong Y., Edwards E.A.;
RT   "Semi-automatic in silico gap closure enabled de novo assembly of two
RT   dehalobacter genomes from metagenomic data.";
RL   PLoS ONE 7:E52038-E52038(2012).
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}.
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DR   EMBL; CP003870; AFV04007.1; -; Genomic_DNA.
DR   RefSeq; WP_015042076.1; NC_018867.1.
DR   EnsemblBacteria; AFV04007; AFV04007; DCF50_p1.
DR   KEGG; dec:DCF50_p1; -.
DR   PATRIC; fig|1131462.4.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000482; 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; 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:UP000000482};
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:UP000000482}.
FT   DOMAIN      140    268       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      352    421       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   445 AA;  50921 MW;  5641B7CE47021A58 CRC64;
     MSPNIIYLNA FWENILEKLK DELSKPSFET WLSSTKLVDF SNNRLTISVS NEFAKDWLES
     RYSSLVKSTV QNYLNAPVTL NFIAEQDPSD LPPIETPGVN FGVLSHSLNP KYTFDTFVIG
     NGNRFAHAAA LAVAESPAKS YNPLFVYGGS GLGKTHLMHA ISHVISKNFP SMKILYVTGE
     QFTNEMIDSI RYERQVEFRN TYRKIDILLI DDIQFLAGKE GTQEEFFHTF NTLYEANKQI
     IISSDRPPRE IPTLEERLRS RFEWGLTTDI NPPDYETRIA ILRKKAELEN FIVPDEIIIF
     IASEIQSNIR ELEGALSKIT AYCMLTNQPI TVTLAEEILK DMIPQKNQKL ISLDMIQKSV
     AEHYKMSVQE FKQKKRTRTI AFPRQIAMFL CREMTDLSLE QIGDKFGGRD HTTVIHACEK
     ISELKKNDPL VEKSINDIIS KIKSS
//
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