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Database: UniProt
Entry: I2EP88_EMTOG
LinkDB: I2EP88_EMTOG
Original site: I2EP88_EMTOG 
ID   I2EP88_EMTOG            Unreviewed;       485 AA.
AC   I2EP88;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   25-OCT-2017, entry version 40.
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=Emtol_0337 {ECO:0000313|EMBL:AFK01491.1};
OS   Emticicia oligotrophica (strain DSM 17448 / GPTSA100-15).
OC   Bacteria; Bacteroidetes; Cytophagia; Cytophagales; Cytophagaceae;
OC   Emticicia.
OX   NCBI_TaxID=929562 {ECO:0000313|EMBL:AFK01491.1, ECO:0000313|Proteomes:UP000002875};
RN   [1] {ECO:0000313|EMBL:AFK01491.1, ECO:0000313|Proteomes:UP000002875}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17448 / GPTSA100-15 {ECO:0000313|Proteomes:UP000002875};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA   Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA   Teshima H., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Tindall B.,
RA   Pomrenke H., Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of chromosome of Emticicia oligotrophica DSM
RT   17448.";
RL   Submitted (JUL-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: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; CP002961; AFK01491.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFK01491; AFK01491; Emtol_0337.
DR   KEGG; eol:Emtol_0337; -.
DR   PATRIC; fig|929562.3.peg.1; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002875; 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:UP000002875};
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:UP000002875}.
FT   DOMAIN      182    312       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      393    462       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     190    197       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   485 AA;  55415 MW;  0403E813C5D593E2 CRC64;
     MTILENPKTP NVTLQREVDI VWQNCLKMIR ESISEQSYKT WFEPIIPAKL EGKKLTIQVP
     SQFFYEWLEE NYVHLLRKSL DYAIGRDGML EYSIVVDSGN RQKNEPQIAV NMPPVHTPQY
     AKPDNPNADV VKNPFQMKDL DSLSLDSYLN PNYTFDNFVE GDCNRLARAA GFAVASKPGV
     TSFNPLMIYG GVGLGKTHLV QAIGNFMKNK AANKFVLYVS SEKFTSQFIN AIKNNSLQDF
     MNFYMQIDIL IIDDVQFLSG KEKTQETFFH IFNHLHQSGR QIVMTSDRPP RELEGVEDRL
     LSRFKWGLTA DLQTPDFETR IAIIQKKVQA EGISIAYEVI EYLAHSIDTN VRELEGVMIS
     LLAQASLTRR EIDLELAKAT LRHLVKDSER EVTVDTIIEA ITEHYKVRTA DLKGKSRLRE
     IVLPRQVAMY LTKELTNLSL KSIGYHFGGR DHSTVIHAIQ TVNDLMDTDK EISSAVNKLL
     KMFRK
//
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