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Database: UniProt
Entry: F5YLH0_TREPZ
LinkDB: F5YLH0_TREPZ
Original site: F5YLH0_TREPZ 
ID   F5YLH0_TREPZ            Unreviewed;       479 AA.
AC   F5YLH0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   25-OCT-2017, entry version 47.
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:AEF84323.1};
GN   OrderedLocusNames=TREPR_0277 {ECO:0000313|EMBL:AEF84323.1};
OS   Treponema primitia (strain ATCC BAA-887 / DSM 12427 / ZAS-2).
OC   Bacteria; Spirochaetes; Spirochaetales; Spirochaetaceae; Treponema.
OX   NCBI_TaxID=545694 {ECO:0000313|EMBL:AEF84323.1, ECO:0000313|Proteomes:UP000009223};
RN   [1] {ECO:0000313|Proteomes:UP000009223}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-887 / DSM 12427 / ZAS-2
RC   {ECO:0000313|Proteomes:UP000009223};
RA   Tetu S.G., Matson E., Ren Q., Seshadri R., Elbourne L., Hassan K.A.,
RA   Durkin A., Radune D., Mohamoud Y., Shay R., Jin S., Zhang X.,
RA   Lucey K., Ballor N.R., Ottesen E., Rosenthal R., Allen A.,
RA   Leadbetter J.R., Paulsen I.T.;
RT   "Complete sequence of Treponema primitia strain ZAS-2.";
RL   Submitted (DEC-2009) 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: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; CP001843; AEF84323.1; -; Genomic_DNA.
DR   RefSeq; WP_015706206.1; NC_015578.1.
DR   STRING; 545694.TREPR_0277; -.
DR   EnsemblBacteria; AEF84323; AEF84323; TREPR_0277.
DR   KEGG; tpi:TREPR_0277; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000009223; 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:UP000009223};
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:UP000009223}.
FT   DOMAIN      170    302       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      382    451       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     178    185       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   479 AA;  54308 MW;  355DC1F87A34854A CRC64;
     MADGDYDLIW KETMSQIQEE LGEQEFAMWF NLEYLGASEN ELTIGVPSLF YLDQVKTRYQ
     LYIEGKIREL IGKNISIVFI IKTRTKEDPV LPPAEGKPVP EFAPTRGTSL QVSRGTSQVT
     PKPIQGVTMA HKKRHPQLRE DYTFDKYVIG DDNNFAANAA QAVAKNPGTA YNPCLIYGSV
     GLGKTHLMQA IGNYIHEGTD NKIIYITAEG FMNEFIQYLG EGKMPAFKNK YRYVDVLLID
     DIHTLGAKGN QTQEELFHTF NALYNDKKQI VFTCDRPVSE LKNLTDRLKS RFSQGLNVDL
     QPPNYETRCA ILKKKVEFQG ISIPDEVITF VSKNISTNVR DLEGALNKLI AYTVLGKKTL
     TLEIAQQQLK DIIHSSKTSQ MSIDIIQRVI AEHYHLSPND LKGRKKTQNI VTPRQLAMYI
     TRELTENSTT EIGQFFGGRD HTTVMHSCQK IEEKIRSDPQ TESLIQTLIR LIKDSSVKS
//
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