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Database: UniProt
Entry: G2LDV0_CHLTF
LinkDB: G2LDV0_CHLTF
Original site: G2LDV0_CHLTF 
ID   G2LDV0_CHLTF            Unreviewed;       464 AA.
AC   G2LDV0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   05-JUL-2017, entry version 44.
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   OrderedLocusNames=Cabther_A0001 {ECO:0000313|EMBL:AEP10781.1};
OS   Chloracidobacterium thermophilum (strain B).
OC   Bacteria; Acidobacteria; Blastocatellia; Chloracidobacterium.
OX   NCBI_TaxID=981222 {ECO:0000313|EMBL:AEP10781.1, ECO:0000313|Proteomes:UP000006791};
RN   [1] {ECO:0000313|EMBL:AEP10781.1, ECO:0000313|Proteomes:UP000006791}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B {ECO:0000313|EMBL:AEP10781.1,
RC   ECO:0000313|Proteomes:UP000006791};
RX   PubMed=21951563; DOI=10.1111/j.1462-2920.2011.02592.x;
RA   Garcia Costas A.M., Liu Z., Tomsho L.P., Schuster S.C., Ward D.M.,
RA   Bryant D.A.;
RT   "Complete genome of Candidatus Chloracidobacterium thermophilum, a
RT   chlorophyll-based photoheterotroph belonging to the phylum
RT   Acidobacteria.";
RL   Environ. Microbiol. 14:177-190(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; CP002514; AEP10781.1; -; Genomic_DNA.
DR   RefSeq; WP_014098519.1; NC_016024.1.
DR   STRING; 981222.Cabther_A0001; -.
DR   EnsemblBacteria; AEP10781; AEP10781; Cabther_A0001.
DR   KEGG; ctm:Cabther_A0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   Proteomes; UP000006791; Chromosome 1.
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:UP000006791};
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:UP000006791}.
FT   DOMAIN      164    292       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      373    442       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     172    179       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   464 AA;  53175 MW;  A6C2135AC121BF9D CRC64;
     MMDDEKWTAF LREIERRINH ESFSTWFKPV TLHACQGDTI YLRVPNRSYE DWITETYHEY
     VEEALKAVGC GGARLVFVYT ESPEPKSANG LLDDESPKSG KDAFSFGVFD SELSEGLAGA
     RIVDLEPLEL PLNPKYTFDT FVVGSCNQFA RAAAMAVADT PTRTYNPLFI YGGVGLGKTH
     LMHAIGHAIR NRDRHMRLVY ISSEKFMNEL INAIRYDKAQ AFREKYRSID VLLIDDIQFI
     AGKERTQEEF FHTFNALYDA QKQIVISSDC PPREIPTLEE RLHSRFEWGL IADLQPPDLE
     TKVAILKRKA DLEKIDLSDN VALFIAGKIK SNIRELEGSL IRLVAYASLK QRPIDIELCK
     EVLNIEEEER PITIEMIQRV VSDHYGLRVA DLKSKNNSRN IAVPRQVAMY LCKQLTNHSL
     PEIGRHFGNK HHTTVLHSCE KISRLYQTQN DFHRLINNLI SSLK
//
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