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Database: UniProt
Entry: E8T2Q5_THEA1
LinkDB: E8T2Q5_THEA1
Original site: E8T2Q5_THEA1 
ID   E8T2Q5_THEA1            Unreviewed;       471 AA.
AC   E8T2Q5;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   25-OCT-2017, entry version 54.
DE   RecName: Full=Chromosomal replication initiator protein DnaA {ECO:0000256|HAMAP-Rule:MF_00377, ECO:0000256|RuleBase:RU000577};
GN   Name=dnaA {ECO:0000256|HAMAP-Rule:MF_00377};
GN   OrderedLocusNames=Theam_0006 {ECO:0000313|EMBL:ADU95980.1};
OS   Thermovibrio ammonificans (strain DSM 15698 / JCM 12110 / HB-1).
OC   Bacteria; Aquificae; Desulfurobacteriales; Desulfurobacteriaceae;
OC   Thermovibrio.
OX   NCBI_TaxID=648996 {ECO:0000313|EMBL:ADU95980.1, ECO:0000313|Proteomes:UP000006362};
RN   [1] {ECO:0000313|EMBL:ADU95980.1, ECO:0000313|Proteomes:UP000006362}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15698 / JCM 12110 / HB-1
RC   {ECO:0000313|Proteomes:UP000006362};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Vetriani C.,
RA   Woyke T.;
RT   "Complete sequence of chromosome of Thermovibrio ammonificans HB-1.";
RL   Submitted (JAN-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:SAAS00747914}.
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; CP002444; ADU95980.1; -; Genomic_DNA.
DR   RefSeq; WP_013536766.1; NC_014926.1.
DR   STRING; 648996.Theam_0006; -.
DR   EnsemblBacteria; ADU95980; ADU95980; Theam_0006.
DR   KEGG; tam:Theam_0006; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235658; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000006362; 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; IPR013317; DnaA.
DR   InterPro; IPR013159; DnaA_C.
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   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.
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:UP000006362};
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:UP000006362}.
FT   DOMAIN      140    268       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      356    425       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     148    155       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  53962 MW;  A3D1662C7A103A64 CRC64;
     MDRAYESFLS ELKKRVKPSL FKSAFKDMKL AERSDERILL QVKDSVLKEV IEKNLRPVVE
     EAAKKVFGPV KVEFTVPSEP VKTPQPQQLE LGLFKKSQKK EEELQSNLNP KYTFENFIVG
     TSNQFAHAAA LAVAENPGKA YNPLFIYGGV GLGKTHLMQA IGNYIKKKSP WKKVIYVTTE
     TFMNQLIEAL KSDNISSFRE KYRNIDVLLI DDIQFIGGKE RTQIEFFHTF NALYDAGKQV
     VLTSDRPPKD IPTLTERLRS RFEWGLIADI QPPDFETRVA ILKRKAELEG IEVSDKVIKL
     IATIIKSNIR QLEGALIKLK AKATLEGKPI TERLVRELFS QESPEERAEK RRREISLKLI
     KTTVSSEFGV DEELLLSSSR KKQVALARQV AMYLAKRIGN YPYTQIAAAF NRDDHTTVLH
     AVRKVEELRK RDEKINQLLE KLELKVREEV ERSSQVIHSD VDNYVDKSVD N
//
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