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Database: UniProt
Entry: D0MJZ7_RHOM4
LinkDB: D0MJZ7_RHOM4
Original site: D0MJZ7_RHOM4 
ID   D0MJZ7_RHOM4            Unreviewed;       503 AA.
AC   D0MJZ7;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   05-JUL-2017, entry version 62.
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=Rmar_0001 {ECO:0000313|EMBL:ACY46910.1};
OS   Rhodothermus marinus (strain ATCC 43812 / DSM 4252 / R-10)
OS   (Rhodothermus obamensis).
OC   Bacteria; Bacteroidetes; Bacteroidetes Order II. Incertae sedis;
OC   Rhodothermaceae; Rhodothermus.
OX   NCBI_TaxID=518766 {ECO:0000313|EMBL:ACY46910.1, ECO:0000313|Proteomes:UP000002221};
RN   [1] {ECO:0000313|EMBL:ACY46910.1, ECO:0000313|Proteomes:UP000002221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43812 / DSM 4252 / R-10
RC   {ECO:0000313|Proteomes:UP000002221};
RX   PubMed=21304669; DOI=10.4056/sigs.46736;
RA   Nolan M., Tindall B.J., Pomrenke H., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F.,
RA   Saunders E., Han C., Bruce D., Goodwin L., Chain P., Pitluck S.,
RA   Ovchinikova G., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P., Detter J.C.;
RT   "Complete genome sequence of Rhodothermus marinus type strain (R-
RT   10).";
RL   Stand. Genomic Sci. 1:283-291(2009).
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: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; CP001807; ACY46910.1; -; Genomic_DNA.
DR   RefSeq; WP_012842522.1; NC_013501.1.
DR   STRING; 518766.Rmar_0001; -.
DR   EnsemblBacteria; ACY46910; ACY46910; Rmar_0001.
DR   KEGG; rmr:Rmar_0001; -.
DR   eggNOG; ENOG4105CI4; Bacteria.
DR   eggNOG; COG0593; LUCA.
DR   HOGENOM; HOG000235659; -.
DR   KO; K02313; -.
DR   OMA; REFNPLF; -.
DR   OrthoDB; POG091H02FF; -.
DR   Proteomes; UP000002221; 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; 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: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.
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:SAAS00731922};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002221};
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:UP000002221}.
FT   DOMAIN      197    406       AAA. {ECO:0000259|SMART:SM00382}.
FT   DOMAIN      408    477       Bac_DnaA_C. {ECO:0000259|SMART:SM00760}.
FT   NP_BIND     205    212       ATP. {ECO:0000256|HAMAP-Rule:MF_00377}.
SQ   SEQUENCE   503 AA;  57915 MW;  2C414D32EC10805B CRC64;
     MERTPEAIWH ACLEIIRDNV NRQSFKTWFE PIKPVSLTEE DDQIKLTVEL PSRFYYEWLE
     EHYYSLLRKT ITKVLGPKGR LFYKIVIEKE DPQSGFEGIS VNMPAHPPET TPPPPPPRTR
     PVSPTAPPIT PESPVEVAEQ EPPVPTNPFA IPGIIRKIQV DSQLDPKYTF ERFIEGDCNR
     LARSAALAIA QQPGATSFNP FLVYGGVGLG KTHLIQAIGN YARQHHTAET IRYVSSEQFT
     NEFVQAIQHN RINEFSLFYR HIDLLIVDDI QFFGGKEKTQ EEFFHIFNAL HQTGKQIVLS
     ADRPPKDIPG IEERLLSRFQ WGLMADVQPP DLETRIAILR RKAEDEGIEL GDDVIEFIAH
     HVKSNFRELE GALLRLVAHA AYQRRDIDLA LAREALRDLI KESRVTLTID QIQQLVCEYF
     DIEPDLIRSK TRKREIVQAR QVAMYFCKQF TQHSLKSIGL HFGGRDHSTV IHACQSVENL
     METDPKFREI IEELRHKISL YSR
//
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