GenomeNet

Database: UniProt
Entry: M1E6J9_9FIRM
LinkDB: M1E6J9_9FIRM
Original site: M1E6J9_9FIRM 
ID   M1E6J9_9FIRM            Unreviewed;       442 AA.
AC   M1E6J9;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-SEP-2017, entry version 34.
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=Thena_0001 {ECO:0000313|EMBL:AEE13654.1};
OS   Thermodesulfobium narugense DSM 14796.
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermodesulfobiaceae; Thermodesulfobium.
OX   NCBI_TaxID=747365 {ECO:0000313|EMBL:AEE13654.1, ECO:0000313|Proteomes:UP000011765};
RN   [1] {ECO:0000313|EMBL:AEE13654.1, ECO:0000313|Proteomes:UP000011765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14796 {ECO:0000313|EMBL:AEE13654.1,
RC   ECO:0000313|Proteomes:UP000011765};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N.,
RA   Ovchinnikova G., Zhang X., Saunders L., Detter J.C., Tapia R., Han C.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Spring S., Schroeder M., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Thermodesulfobium narugense DSM 14796.";
RL   Submitted (APR-2011) 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:SAAS00756131}.
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; CP002690; AEE13654.1; -; Genomic_DNA.
DR   STRING; 747365.Thena_0001; -.
DR   EnsemblBacteria; AEE13654; AEE13654; Thena_0001.
DR   KEGG; tnr:Thena_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000011765; 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: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:UP000011765};
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:UP000011765}.
FT   DOMAIN      137    265       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      350    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     145    152       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   442 AA;  50566 MW;  3D0317AECD32E0F9 CRC64;
     MNNIWQEILD VVEEKMGKPT VEAFLKPSRA IINKEDNKLT LIVPNEFIKT YIEQKSGKLK
     NIIEDILEGE NLKLSLEVDE SIGNLSQEEY LENNNKVEKN EQKGFLSKYT FETFVVGPGN
     RMAHAASLAV ADNPGKAYNP LFIYGGAGLG KTHLLQAIAT TIRSKKPNLY ILYITSEKFT
     NEFINAIKDD KINSFQEHYR NIDILLVDDI QFIAGKERTQ EEFFHTFNTL YESGKQIVLS
     SDRPPKEIRT LEERLRTRFE MGLIADIQPP DLETRIAILQ KKAEIENIDI DPEALVLIAE
     KVASNIRELE GVLTKSMALC SINQESRITI KHAQEALKNI EDNKLNNLPT MDEIAIAVSK
     VMQIKLEDLK SRGRKSHQAN ARQIAMYLCR EMTKNSLPQI GEYFGRDHST VIHAYERIKE
     DINKDQTLKR IIEQIRSFLK SV
//
DBGET integrated database retrieval system