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Database: UniProt
Entry: D4M1B8_9FIRM
LinkDB: D4M1B8_9FIRM
Original site: D4M1B8_9FIRM 
ID   D4M1B8_9FIRM            Unreviewed;       456 AA.
AC   D4M1B8;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   16-JAN-2019, entry version 61.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01081161};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   ORFNames=RTO_02470 {ECO:0000313|EMBL:CBL25030.1};
OS   [Ruminococcus] torques L2-14.
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Lachnospiraceae;
OC   Blautia.
OX   NCBI_TaxID=657313 {ECO:0000313|EMBL:CBL25030.1, ECO:0000313|Proteomes:UP000008956};
RN   [1] {ECO:0000313|EMBL:CBL25030.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25030.1,
RC   ECO:0000313|Proteomes:UP000008956};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Ruminococcus torques L2-14.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL25030.1, ECO:0000313|Proteomes:UP000008956}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L2-14 {ECO:0000313|EMBL:CBL25030.1,
RC   ECO:0000313|Proteomes:UP000008956};
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:SAAS00756121}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
CC       ECO:0000256|SAAS:SAAS01082709}.
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; FP929055; CBL25030.1; -; Genomic_DNA.
DR   ProteinModelPortal; D4M1B8; -.
DR   STRING; 657313.RTO_02470; -.
DR   EnsemblBacteria; CBL25030; CBL25030; RTO_02470.
DR   KEGG; rto:RTO_02470; -.
DR   PATRIC; fig|657313.3.peg.1986; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   Proteomes; UP000008956; 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   Gene3D; 3.30.300.180; -; 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; IPR038454; DnaA_N_sf.
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:SAAS00756129};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008956};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS01082702};
KW   DNA replication {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU004227, ECO:0000256|SAAS:SAAS00756116};
KW   DNA-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS01082706};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00756117};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008956}.
FT   DOMAIN      142    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      363    432       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     150    157       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
FT   COILED      313    333       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   456 AA;  51682 MW;  600A47BC6FCB381D CRC64;
     MNIVEQNWDQ VLNKMKLEYC SSNISYTTWI APLTVYEVKD NTVYILVKLK ASLEHIQDKY
     LLPFKVCIAE VTGTEYEVEF VTDSPKVIKE KKESSVQKTR VNAIYEKANL NPKYTFDTFV
     VGSNNNFAHA ASLAVAESPG EIYNPLFLYG GVGLGKTHLM HSVAHYILEH DPSKKVLYVT
     SETFTNELID ALKVGKNGNE LAMTTFREKY RNNDVLLIDD IQFIIGKEST QEEFFHTFNH
     LHVSGKQIII SSDKPPKDIE TLEARLRTRF EWGLIADISS PDYETRMAIL RKKEELDGLE
     KYHIPDEVMQ YIANNIKSNI RELEGSLNKL IALSNLENKP IDIPLAAEAL KDMISPDDTR
     AVSPELIMDV VSEHFNVPVT ELKGKKRNAE IVLPRQIVMY LCRNMTDTPL KSIGALLGGK
     DHASISHGVR KIENDLKTDE ALNNTVNIIK KKINPV
//
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