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Database: UniProt
Entry: M4V897_9DELT
LinkDB: M4V897_9DELT
Original site: M4V897_9DELT 
ID   M4V897_9DELT            Unreviewed;       464 AA.
AC   M4V897;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-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   ORFNames=A11Q_1 {ECO:0000313|EMBL:AGH94221.1};
OS   Bdellovibrio exovorus JSS.
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Bdellovibrionales;
OC   Bdellovibrionaceae; Bdellovibrio.
OX   NCBI_TaxID=1184267 {ECO:0000313|EMBL:AGH94221.1, ECO:0000313|Proteomes:UP000012040};
RN   [1] {ECO:0000313|EMBL:AGH94221.1, ECO:0000313|Proteomes:UP000012040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JSS {ECO:0000313|EMBL:AGH94221.1};
RX   PubMed=23190728; DOI=10.1038/ismej.2012.149;
RA   Pasternak Z., Pietrokovski S., Rotem O., Gophna U.,
RA   Lurie-Weinberger M.N., Jurkevitch E.;
RT   "By their genes ye shall know them: genomic signatures of predatory
RT   bacteria.";
RL   ISME J. 7:756-769(2013).
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; CP003537; AGH94221.1; -; Genomic_DNA.
DR   RefSeq; WP_015468711.1; NC_020813.1.
DR   EnsemblBacteria; AGH94221; AGH94221; A11Q_1.
DR   KEGG; bex:A11Q_1; -.
DR   PATRIC; fig|1184267.3.peg.1; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000012040; 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:UP000012040};
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:UP000012040}.
FT   DOMAIN      158    287       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      368    437       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     166    173       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  53258 MW;  7C2C890DFF54F7B8 CRC64;
     MELDSLFWNQ IKTTIKTKNG ANKLLENWLD PIELIKSEKT ADSLKITFGV PSQFFFFYVN
     EHLKDKIAQE LREQSNIPVE IDFVVTGKTA SDYNTSLQDV MQNTEQVFQQ PVQVVPAGPR
     PVENINEEFT FSTFVVGKNS EFAHAATYNV ACNPGTNDYN PLLIYGPSGM GKTHLLNAAG
     NQIRQNYPHL RIVYISAERF LNECVSALRR HEMDKFRQKY RENTDVIVVD DVQYIGRGEA
     VQEEFFHMIN SFIEKKKQVV LASDRMPKDI LGLEDRSRTR LERGLIADIT MPDLETRLAI
     LRYKAENYNV RLNEDTIQYI AKISKKSIRE LEGNLKKIKM FSELQGLSIN LELARKVLAH
     HENTVTISIE EIQRIVAEYY KIRVTDLKST SRAKPIVVPR QIAMYLIKKF LDKSLVDIGK
     AFGGKDHTTV INSLDKVENL QNQDPQFKND IDELINQIHN VTGL
//
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