ID A0A1J0LV14_THEBO Unreviewed; 267 AA.
AC A0A1J0LV14;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=A0O31_01748 {ECO:0000313|EMBL:APD09844.1};
OS Thermus brockianus.
OC Bacteria; Deinococcota; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=56956 {ECO:0000313|EMBL:APD09844.1, ECO:0000313|Proteomes:UP000182993};
RN [1] {ECO:0000313|Proteomes:UP000182993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE-1 {ECO:0000313|Proteomes:UP000182993};
RA Schaefers C., Blank S., Wiebusch S., Elleuche S., Antranikian G.;
RT "Whole genome sequencing of Thermus brockianus strain GE-1.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016312; APD09844.1; -; Genomic_DNA.
DR RefSeq; WP_071677492.1; NZ_CP016312.1.
DR AlphaFoldDB; A0A1J0LV14; -.
DR STRING; 56956.A0O31_01748; -.
DR KEGG; tbc:A0O31_01748; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000182993; 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; 29064 MW; A44B4537543520BA CRC64;
MKARAIVVTS GKGGVGKTTT TANLGAALAK LGEKVAVVDV DVGLRNLDVV MGLEGRVVFD
LIDVLEGRAK PRQALIRDKR VENLYLLPAS QTKDKEALDP AKFRELIQLL LNEEGFDRVL
IDSPAGIEKG FQTAATPAEG ALVVVNPEVS SVRDADRIIG LLEAREIREN YLIVNRLRPK
MVSRGDMLSV EDVVEILGLK PIGIIPEDEQ VIVSTNQGEP LVLKGTSPAA QAFLDTARRM
RGEEVPFRHL DEVQGFLGVL RRLFGGR
//
