ID H9ZQU8_THETH Unreviewed; 267 AA.
AC H9ZQU8;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN ORFNames=TtJL18_0805 {ECO:0000313|EMBL:AFH38708.1};
OS Thermus thermophilus JL-18.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=798128 {ECO:0000313|EMBL:AFH38708.1, ECO:0000313|Proteomes:UP000007388};
RN [1] {ECO:0000313|EMBL:AFH38708.1, ECO:0000313|Proteomes:UP000007388}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JL-18 {ECO:0000313|EMBL:AFH38708.1,
RC ECO:0000313|Proteomes:UP000007388};
RX PubMed=23405355; DOI=10.1128/genomeA.00106-12;
RA Murugapiran S.K., Huntemann M., Wei C.L., Han J., Detter J.C., Han C.S.,
RA Erkkila T.H., Teshima H., Chen A., Kyrpides N., Mavrommatis K.,
RA Markowitz V., Szeto E., Ivanova N., Pagani I., Lam J., McDonald A.I.,
RA Dodsworth J.A., Pati A., Goodwin L., Peters L., Pitluck S., Woyke T.,
RA Hedlund B.P.;
RT "Whole Genome Sequencing of Thermus oshimai JL-2 and Thermus thermophilus
RT JL-18, Incomplete Denitrifiers from the United States Great Basin.";
RL Genome Announc. 1:E00106-E00112(2013).
CC -!- FUNCTION: ATPase required for the correct placement of the division
CC site. Cell division inhibitors MinC and MinD act in concert to form an
CC inhibitor capable of blocking formation of the polar Z ring septums.
CC Rapidly oscillates between the poles of the cell to destabilize FtsZ
CC filaments that have formed before they mature into polar Z rings.
CC {ECO:0000256|ARBA:ARBA00025436}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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DR EMBL; CP003252; AFH38708.1; -; Genomic_DNA.
DR RefSeq; WP_011173307.1; NC_017587.1.
DR AlphaFoldDB; H9ZQU8; -.
DR STRING; 798128.TtJL18_0805; -.
DR GeneID; 3168976; -.
DR KEGG; ttl:TtJL18_0805; -.
DR PATRIC; fig|798128.4.peg.783; -.
DR HOGENOM; CLU_037612_0_1_0; -.
DR Proteomes; UP000007388; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02036; MinD; 1.
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; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR01968; minD_bact; 1.
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 PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 6..221
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 267 AA; 28890 MW; 0F11E05CC41F979D CRC64;
MKARAIVVTS GKGGVGKTTT TANLGAALAK LGEKVAVVDV DVGLRNLDVV MGLEGRVVFD
LVDVLEGRAR LRQALIRDKR VENLFLLPAS QTKDKEALDP ERFKEVVRAL LEEEGFDRVL
IDSPAGIEKG FQTAAAPAEG ALVVVNPEVS SVRDADRIIG LLEAREVREN FLVINRLRPR
MVARGDMLSV EDVVEILGLK PIGIIPEDEQ VIVSTNQGEP LVLKGTGPAA QAYMDTARRL
RGEEVPFRAL EDAQGLLGVL KRLFGGR
//
