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Database: UniProt
Entry: D4MRD5_9FIRM
LinkDB: D4MRD5_9FIRM
Original site: D4MRD5_9FIRM 
ID   D4MRD5_9FIRM            Unreviewed;       456 AA.
AC   D4MRD5;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   20-DEC-2017, entry version 53.
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   ORFNames=CL3_18520 {ECO:0000313|EMBL:CBL36321.1};
OS   butyrate-producing bacterium SM4/1.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales.
OX   NCBI_TaxID=245012 {ECO:0000313|EMBL:CBL36321.1, ECO:0000313|Proteomes:UP000008959};
RN   [1] {ECO:0000313|EMBL:CBL36321.1, ECO:0000313|Proteomes:UP000008959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36321.1,
RC   ECO:0000313|Proteomes:UP000008959};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Clostridiales sp. SM4/1.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL36321.1, ECO:0000313|Proteomes:UP000008959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SM4/1 {ECO:0000313|EMBL:CBL36321.1,
RC   ECO:0000313|Proteomes:UP000008959};
RA   Pajon A.;
RL   Submitted (MAR-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:SAAS00735475}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS00911680}.
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; FP929060; CBL36321.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4MRD5; -.
DR   EnsemblBacteria; CBL36321; CBL36321; CL3_18520.
DR   KEGG; bprm:CL3_18520; -.
DR   PATRIC; fig|245012.3.peg.1315; -.
DR   KO; K02313; -.
DR   Proteomes; UP000008959; Chromosome.
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; IPR027417; P-loop_NTPase.
DR   InterPro; IPR010921; Trp_repressor/repl_initiator.
DR   PANTHER; PTHR30050:SF2; PTHR30050:SF2; 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:SAAS00747950};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00911664};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00747996};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00911684};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008959}.
FT   DOMAIN      148    280       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    432       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      432    452       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   456 AA;  52092 MW;  75A33CB5212B3316 CRC64;
     MLEKIKEKWE DILLHIKEEH ELTDVSFKTW LLPTEAYSMK GNTLQILVPD IHFLGYMQKK
     YGFLLTVAIA EITGIECQVD FITREQIKEE PEEVSENQLL SHSTDVDQQV IQNANLNPRY
     TFDTFVVGAN NNLAHAASLA VAESPGEIYN PLFIYGGVGL GKTHLMHSIG HFILQNNPKA
     KILYVTSEKF TNELIDAIRN KNNISTTEFR EKYRNNDVLL IDDIQFIIGK ESTQEEFFHT
     FNALYEAKKQ IIISSDKPPK EIETLEERLR SRFEWGLTVD IQSPDYETRM AILRKKEELE
     GYNIDNEVIK YIATHVKSNI RELEGALTKI VALSKLNKRE ITTELAEEAL KDLISPGGAR
     EITPELIIQV VSDHFGITPA DISSKKRNKE IVYPRQIAMY LCRTMTGTPL QGIGKYLGDR
     DHTTIIHGAE KITADMEKNE SLRNTIEVLK KKLSPQ
//
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