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Database: UniProt
Entry: F4LR73_TEPAE
LinkDB: F4LR73_TEPAE
Original site: F4LR73_TEPAE 
ID   F4LR73_TEPAE            Unreviewed;       453 AA.
AC   F4LR73;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   25-OCT-2017, entry version 51.
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:CDI40249.1};
GN   OrderedLocusNames=TEPIRE1_0001 {ECO:0000313|EMBL:CDI40249.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CDI40249.1, ECO:0000313|Proteomes:UP000010802};
RN   [1] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(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: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; HF563609; CDI40249.1; -; Genomic_DNA.
DR   RefSeq; WP_013777140.1; NC_019954.2.
DR   EnsemblBacteria; CDI40249; CDI40249; TepiRe1_0001.
DR   KEGG; tae:TepiRe1_0001; -.
DR   KEGG; tep:TepRe1_0001; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000010802; 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:UP000010802};
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:UP000010802}.
FT   DOMAIN      148    276       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      360    429       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     156    163       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   453 AA;  51244 MW;  F54F33C3CB1EBC7D CRC64;
     MSIDPLYLWQ HVLKILSNEL NNDMSFNTVL KPTRLAALEA DTAIVEVPND FIKSVIEKRY
     LNLIKDIFSS VLKQNINVVI NVNPEGFGSE VLPDDSISLN EVSETKTLAE DTTPSLNQKY
     TFDTFVVGNS NRFAHAASQA VAQAPAKAYN PFFIYGGVGL GKTHLMHAIG HYILQQDPTC
     KVVYLSSEKF TNELINSIRD DKNVEFRNKY RTIDVLLIDD IQFIAGKERT QEEFFHTFNA
     LHDANKQLVI SSDRPPKEIP TLEERLRSRF EWGLITDIQP PDFETRIAIL QKKAMMENLI
     VPNDVINFIA TKIETNIREL EGALIRVVAY SSLTDCPIDI GLAEQVLKDI LPDGKPKQVT
     SKQIVEEVGS YFSISPEEFK SKKRTKDLAF ARQVAMYLCC ELTDLSLPKI GEEFGGRDHT
     TVIHARDKIT RDIQEDSQLS NAVESLKKKI LYS
//
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