GenomeNet

Database: UniProt
Entry: W6RU88_9CLOT
LinkDB: W6RU88_9CLOT
Original site: W6RU88_9CLOT 
ID   W6RU88_9CLOT            Unreviewed;       449 AA.
AC   W6RU88;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   25-OCT-2017, entry version 29.
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:CDM67199.1};
GN   ORFNames=CM240_0001 {ECO:0000313|EMBL:CDM67199.1};
OS   Clostridium bornimense.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1216932 {ECO:0000313|EMBL:CDM67199.1, ECO:0000313|Proteomes:UP000019426};
RN   [1] {ECO:0000313|EMBL:CDM67199.1, ECO:0000313|Proteomes:UP000019426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2/40 {ECO:0000313|Proteomes:UP000019426};
RA   Wibberg D., Puehler A., Schlueter A.;
RT   "Complete genome sequence of Clostridum sp. M2/40.";
RL   Submitted (NOV-2013) 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:SAAS00911680}.
CC   -!- SIMILARITY: Belongs to the DnaA family. {ECO:0000256|HAMAP-
CC       Rule:MF_00377, ECO:0000256|RuleBase:RU004227,
CC       ECO:0000256|SAAS:SAAS00555179}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; HG917868; CDM67199.1; -; Genomic_DNA.
DR   RefSeq; WP_044035683.1; NZ_HG917868.1.
DR   EnsemblBacteria; CDM67199; CDM67199; CM240_0001.
DR   KEGG; clt:CM240_0001; -.
DR   PATRIC; fig|1216932.3.peg.1; -.
DR   KO; K02313; -.
DR   Proteomes; UP000019426; 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; IPR024633; DnaA_N_dom.
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   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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000019426};
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:UP000019426}.
FT   DOMAIN      142    270       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    423       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   449 AA;  50908 MW;  8017D81518364766 CRC64;
     MKVQLDDLWA KTLEIMQNEL TEVSFNTWIK SICPIEITGD TIKLSVPNDF TREILEGRYK
     DLLINAIKVA TNKEYKIEFL IGSEEAITKS ETPKQNIVMS SPADGMQAVL NPKYTFDSFV
     IGNSNRFAHA ASLAVSESPA KAYNPLFIYG GVGLGKTHLM HAIGHYILNK NPKARVAYIS
     SEKFTNELIN SIKDDTNEEF RSKYRNVDVL LIDDIQFIAG KERTQEEFFH TFNALHDANK
     QIILSSDRPP KEIPTLEDRL RSRFEWGLIA DIQPPDFETR IAILKKKADE ENLDIPNDVL
     GYIANTIKSN IRELEGALIR IVAFSSLTNK EISVDLALLA LRDIIANRSS KAITIEYIQE
     MVANYFNVTV EDLKSARRTK SITYPRQIAM YLCRKNTDNS LPKIGEEFGG RDHTTVIHAY
     EKISDALNKD KDPLLKSDIE SLSKKLNKK
//
DBGET integrated database retrieval system