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Database: UniProt
Entry: L0A2L7_DEIPD
LinkDB: L0A2L7_DEIPD
Original site: L0A2L7_DEIPD 
ID   L0A2L7_DEIPD            Unreviewed;       448 AA.
AC   L0A2L7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   05-JUL-2017, entry version 33.
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=Deipe_1939 {ECO:0000313|EMBL:AFZ67442.1};
OS   Deinococcus peraridilitoris (strain DSM 19664 / LMG 22246 / CIP 109416
OS   / KR-200).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales;
OC   Deinococcaceae; Deinococcus.
OX   NCBI_TaxID=937777 {ECO:0000313|EMBL:AFZ67442.1, ECO:0000313|Proteomes:UP000010467};
RN   [1] {ECO:0000313|Proteomes:UP000010467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19664 / LMG 22246 / CIP 109416 / KR-200
RC   {ECO:0000313|Proteomes:UP000010467};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N.,
RA   Lu M., Kyrpides N., Mavromatis K., Ivanova N., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Markowitz V.,
RA   Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Pukall R., Steenblock K.,
RA   Brambilla E., Klenk H.-P., Eisen J.A.;
RT   "Complete sequence of chromosome of Deinococcus peraridilitoris DSM
RT   19664.";
RL   Submitted (MAR-2012) 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}.
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; CP003382; AFZ67442.1; -; Genomic_DNA.
DR   EnsemblBacteria; AFZ67442; AFZ67442; Deipe_1939.
DR   KEGG; dpd:Deipe_1939; -.
DR   PATRIC; fig|937777.3.peg.1944; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000010467; Chromosome.
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; 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.
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:UP000010467};
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:UP000010467}.
FT   DOMAIN      143    271       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      354    422       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     151    158       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  50547 MW;  AA360C832A6A1265 CRC64;
     MLTHVRKNIS EVEYHTWFVP VRPLGVQDGA LVLGVRNSFA QEWFRKHYQD LLEDALRQLG
     ASSPQVSFEV LPAVQDAMMA PATEPNPSSS RRTNPPQVVQ TTSGTGSAKA LNPKYIFENF
     VVGPNNNLAH AAALAVAESP GKTYNPLFVY GDVGLGKTHL MHAVGHYVLE RHPEKRVEYV
     STESFTNDLI NAIREDRMTQ FRNRYRSVDL LLVDDIQFLA GKERTQEEFF HTFNALYESH
     KQIILSSDRP PRDIQTLESR LRSRFEWGLI TDIQSPEFET RVAILKMNAE HRRINIPQEV
     LELIARQVTS NIRELEGALV RVMAFSSLNN VSLSKAVAAK ALSDVFTSQE VQIEMADVLR
     AVAAHFSVPL EALRGSGRVR EVVVPRQIAM YLIRDLTGHS LPEVGVFFGR DHSTVLHATQ
     KVSEQLGRDP ELSTHIETLR RRLQGIEE
//
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