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Database: UniProt
Entry: F8EWL0_TRECH
LinkDB: F8EWL0_TRECH
Original site: F8EWL0_TRECH 
ID   F8EWL0_TRECH            Unreviewed;       471 AA.
AC   F8EWL0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   28-MAR-2018, entry version 50.
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=Spica_0001 {ECO:0000313|EMBL:AEJ18173.1};
OS   Treponema caldarium (strain ATCC 51460 / DSM 7334 / H1) (Spirochaeta
OS   caldaria).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=744872 {ECO:0000313|EMBL:AEJ18173.1, ECO:0000313|Proteomes:UP000000503};
RN   [1] {ECO:0000313|Proteomes:UP000000503}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 51460 / DSM 7334 / H1 {ECO:0000313|Proteomes:UP000000503};
RX   PubMed=23961314; DOI=10.4056/sigs.3096473;
RA   Abt B., Goker M., Scheuner C., Han C., Lu M., Misra M., Lapidus A.,
RA   Nolan M., Lucas S., Hammon N., Deshpande S., Cheng J.F., Tapia R.,
RA   Goodwin L.A., Pitluck S., Liolios K., Pagani I., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Huntemann M., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Rohde M.,
RA   Spring S., Gronow S., Detter J.C., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Woyke T., Klenk H.P.;
RT   "Genome sequence of the thermophilic fresh-water bacterium Spirochaeta
RT   caldaria type strain (H1(T)), reclassification of Spirochaeta
RT   caldaria, Spirochaeta stenostrepta, and Spirochaeta zuelzerae in the
RT   genus Treponema as Treponema caldaria comb. nov., Treponema
RT   stenostrepta comb. nov., and Treponema zuelzerae comb. nov., and
RT   emendation of the genus Treponema.";
RL   Stand. Genomic Sci. 8:88-105(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:SAAS00747961}.
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; CP002868; AEJ18173.1; -; Genomic_DNA.
DR   RefSeq; WP_013967486.1; NC_015732.1.
DR   STRING; 744872.Spica_0001; -.
DR   EnsemblBacteria; AEJ18173; AEJ18173; Spica_0001.
DR   KEGG; scd:Spica_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   BioCyc; TCAL744872:G1GZ2-1-MONOMER; -.
DR   Proteomes; UP000000503; 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:SAAS00747950};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000503};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|SAAS:SAAS00747973};
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:SAAS00748008};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00377,
KW   ECO:0000256|RuleBase:RU000577, ECO:0000256|SAAS:SAAS00747895};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000503}.
FT   DOMAIN      163    292       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      374    443       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     171    178       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   471 AA;  54333 MW;  292AD247766ADA2B CRC64;
     MAIWDYEIFW KETLNQLQQE LEEVEFSLWF NIHYLRSEEN TIIIGVPSSF YRDQFKIRYH
     NLIEEKLHEL SGQPITLQYE VVSKKVIDQE TTFSSQTSQR PSISAKDTTS KSLNQNTLNT
     SIQQKDPHPL LRRDYTFSNY VIGDNNSFAA NAALAISKNP GTAYNPFLVY GGVGLGKTHL
     MQAIGNYIHE HSNAKIIYIT AETFTNEFVQ ALQANKTAAF KNKYRFVDVL LVDDIHFLQN
     KIETQEELFH TFNALYDANK QMVFTCDRPV SELKHLSDRL KSRFERGLTV DLQPPDYETR
     LAILKKKADA RNITIPHEVL ELVSKNISSN VRDLEAALTK LIAYTELVQK PITIEVAQQH
     LKDVFASPKQ ANMSIEAIQR VVAEYFSLSY NDLKGKKRTQ NIVLPRQIAM YIAREITEYS
     TTELGLEFGG RDHTTVMHAC QKIEERIRSD PTLEPIIQNL IRQIKDYRTK N
//
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