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Database: UniProt
Entry: D2NS84_ROTMD
LinkDB: D2NS84_ROTMD
Original site: D2NS84_ROTMD 
ID   D2NS84_ROTMD            Unreviewed;       565 AA.
AC   D2NS84;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 48.
DE   SubName: Full=Septum formation inhibitor-activating ATPase {ECO:0000313|EMBL:BAI64510.1};
GN   OrderedLocusNames=RMDY18_06780 {ECO:0000313|EMBL:BAI64510.1};
OS   Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Rothia.
OX   NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64510.1, ECO:0000313|Proteomes:UP000001883};
RN   [1] {ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA   Fukushima H.;
RT   "Complete genome sequence of Rothia mucilaginosa DJ.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:BAI64510.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64510.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA   Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT   "Isolation and identification of Rothia mucilaginosa from persistent apical
RT   periodontitis lesions.";
RL   J Osaka Dent Univ 44:93-98(2010).
RN   [3] {ECO:0000313|EMBL:BAI64510.1, ECO:0000313|Proteomes:UP000001883}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY-18 {ECO:0000313|EMBL:BAI64510.1,
RC   ECO:0000313|Proteomes:UP000001883};
RA   Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA   Fukushima H.;
RT   "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT   with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT   Lesion.";
RL   Sequencing 2010:457236-457236(2010).
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DR   EMBL; AP011540; BAI64510.1; -; Genomic_DNA.
DR   RefSeq; WP_012903219.1; NC_013715.1.
DR   AlphaFoldDB; D2NS84; -.
DR   STRING; 680646.RMDY18_06780; -.
DR   KEGG; rmu:RMDY18_06780; -.
DR   eggNOG; COG0455; Bacteria.
DR   HOGENOM; CLU_019561_0_0_11; -.
DR   Proteomes; UP000001883; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43384:SF6; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR   Pfam; PF01656; CbiA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000001883}.
FT   DOMAIN          296..533
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   565 AA;  59617 MW;  93E8D6470041BE01 CRC64;
     MNIPVILYGD DGSLLNRIES QRGRVSVART VQDFSEAVGM AHTGIARVLL CAHVPAEISA
     STVDALAASE VLLAVIAPDN LHLPTQAHRI RPEAALDEIL GSLEQAVDAA LARPAAGYGI
     PAQTPNQAPA QAVHQPEAHA AYGQDAGYGY DAGYGYDSGY NGYGYDNGAA GYGVDGYGAG
     GYGYDPAAGA GSNTAAPYGA DYGSYGIDPA VPAGNAPGAP GVHDPAEASS VAPSNEESVL
     SQAAAIVDSF APGSDYALHV QNENNDGTLP QHPDINQDPA APSRYQPGHR LGTIVTVWGT
     HGAPGRSTIA FNLAALAAQQ GQQVCLIDAD TYAPSLDALM ALEDTGSGLA ILCSDADRAQ
     LDEKKAGAIM ERVPLKNGTF DFLSGITSSS RWPEVRARAF AEVLEWLKHR YDLVICDVAA
     PIEVDEELTF DGPAPRRNAA TLTALACADR VIALGEADVI GLPRLINLAR EVQSRPDLFA
     PETDVQYWLN RSRREAAGFN PEAKMRDNWA RYLSVPLTGV IPYERKVMDR LRRNGEALLE
     VAPRHAVVQS LEAMLEGMYA VRAGA
//
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