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Database: UniProt
Entry: F2NNF6_MARHT
LinkDB: F2NNF6_MARHT
Original site: F2NNF6_MARHT 
ID   F2NNF6_MARHT            Unreviewed;       448 AA.
AC   F2NNF6;
DT   31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   31-MAY-2011, sequence version 1.
DT   05-JUL-2017, entry version 43.
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=Marky_0001 {ECO:0000313|EMBL:AEB10766.1};
OS   Marinithermus hydrothermalis (strain DSM 14884 / JCM 11576 / T1).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae;
OC   Marinithermus.
OX   NCBI_TaxID=869210 {ECO:0000313|EMBL:AEB10766.1, ECO:0000313|Proteomes:UP000007030};
RN   [1] {ECO:0000313|EMBL:AEB10766.1, ECO:0000313|Proteomes:UP000007030}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14884 / JCM 11576 / T1 {ECO:0000313|Proteomes:UP000007030};
RX   PubMed=22675595; DOI=10.4056/sigs.2435521;
RA   Copeland A., Gu W., Yasawong M., Lapidus A., Lucas S., Deshpande S.,
RA   Pagani I., Tapia R., Cheng J.F., Goodwin L.A., Pitluck S., Liolios K.,
RA   Ivanova N., Mavromatis K., Mikhailova N., Pati A., Chen A.,
RA   Palaniappan K., Land M., Pan C., Brambilla E.M., Rohde M.,
RA   Tindall B.J., Sikorski J., Goker M., Detter J.C., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA   Woyke T.;
RT   "Complete genome sequence of the aerobic, heterotroph Marinithermus
RT   hydrothermalis type strain (T1(T)) from a deep-sea hydrothermal vent
RT   chimney.";
RL   Stand. Genomic Sci. 6:21-30(2012).
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; CP002630; AEB10766.1; -; Genomic_DNA.
DR   RefSeq; WP_013702821.1; NC_015387.1.
DR   STRING; 869210.Marky_0001; -.
DR   EnsemblBacteria; AEB10766; AEB10766; Marky_0001.
DR   KEGG; mhd:Marky_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000007030; 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:UP000007030};
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:UP000007030}.
FT   DOMAIN      146    274       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      357    426       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     154    161       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   448 AA;  51089 MW;  F6172BC83218C27A CRC64;
     MEGCRGVGTL TQESIWQNVL SYIRNNITEV EYHTWFERIR PLGIQGGVLE LGVPTSFAGE
     WIKKHYADLI QEALLHLGAT SPRFELKVVP GTPVQEDIFS VSTQSQAREN RHKLNPKYTF
     ENFVVGANNN MAHAAALAVA ESPGRAYNPL FIYGGVGLGK THLMHAVGHY VAQRFPHLKI
     EYVSTETFTN ELINAIREDK MSEFRERYRS VDLLLVDDIQ FIAGKERTQE EFFHTFNALY
     EAHKQIILSS DRPPKDILTL ESRLRSRFEW GLITDIQPPE LETRIAILKM NAEYRGISIP
     EEVLEYIARQ ITSNIRELEG ALMRLIAYAS LNGVEITKQV AARALSDVFT PKEAEYKAED
     ILRVVAAHYG VRPEELRGRG RSKEVVLPRQ VAMYLIRELT GASLPEIGQF FQGRDHTTVL
     YAIQKVQELR EQDPAMRQLL RELQEQLG
//
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