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Database: UniProt
Entry: K4LQA5_THEPS
LinkDB: K4LQA5_THEPS
Original site: K4LQA5_THEPS 
ID   K4LQA5_THEPS            Unreviewed;       443 AA.
AC   K4LQA5;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   05-JUL-2017, entry version 36.
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:AFV10259.1};
GN   OrderedLocusNames=Tph_c00010 {ECO:0000313|EMBL:AFV10259.1};
OS   Thermacetogenium phaeum (strain ATCC BAA-254 / DSM 12270 / PB).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermacetogenium.
OX   NCBI_TaxID=1089553 {ECO:0000313|EMBL:AFV10259.1, ECO:0000313|Proteomes:UP000000467};
RN   [1] {ECO:0000313|EMBL:AFV10259.1, ECO:0000313|Proteomes:UP000000467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-254 / DSM 12270 / PB
RC   {ECO:0000313|Proteomes:UP000000467};
RX   PubMed=23259483; DOI=10.1186/1471-2164-13-723;
RA   Oehler D., Poehlein A., Leimbach A., Muller N., Daniel R.,
RA   Gottschalk G., Schink B.;
RT   "Genome-guided analysis of physiological and morphological traits of
RT   the fermentative acetate oxidizer Thermacetogenium phaeum.";
RL   BMC Genomics 13:723-723(2012).
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}.
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DR   EMBL; CP003732; AFV10259.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFV10259; AFV10259; Tph_c00010.
DR   KEGG; tpz:Tph_c00010; -.
DR   KO; K02313; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000000467; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003688; F:DNA replication origin binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006270; P:DNA replication initiation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP.
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:UP000000467};
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:UP000000467}.
FT   DOMAIN      137    265       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      349    418       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     145    152       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   443 AA;  51000 MW;  BF1D7D6A99B6F7B2 CRC64;
     MALGLLRNKL SEIWKDVLEI LQQEVDEHNY SVWLNAASPL AYHDGTLIIL THNDFSREWL
     ETRFSTLIRS RLEYKYNRSF SLRFVTPDSR ENILLPSRGE NQPSLNPKYT FDTFVVGNSN
     RLAHAAALAV AEAPSKAYNP LFIYGGVGLG KTHLMHAIGH HVLKNNRNFR VVYVSSETFT
     NELINAIKDD QNIEFRNKFR NVDVLLVDDI QFLAGKERTQ EEFFHTFNTL HEANKQIIIS
     SDRTPKEIPT LEDRLRSRFE WGLLADIQPP DLETREAILR KKAQLENRVV PDEVIRFIAS
     KIKSNIRELE GALLRVIAYA SLHQKEITLD LSKEALKDLF AGSRKQNITI GLIQRVVAKH
     FNLKVEDLKS KRRTQDVAFP RQIAMYLARE LTEDSLPVIG REFGGRDHTT VMHACDKIKD
     RIQQDINTED TINKLIDMIK TSS
//
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