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Database: UniProt
Entry: A0A1I6QKR6_9BACI
LinkDB: A0A1I6QKR6_9BACI
Original site: A0A1I6QKR6_9BACI 
ID   A0A1I6QKR6_9BACI        Unreviewed;       265 AA.
AC   A0A1I6QKR6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
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=SAMN04488145_1011056 {ECO:0000313|EMBL:SFS53054.1};
OS   Bacillus sp. 103mf.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1761751 {ECO:0000313|EMBL:SFS53054.1, ECO:0000313|Proteomes:UP000198993};
RN   [1] {ECO:0000313|EMBL:SFS53054.1, ECO:0000313|Proteomes:UP000198993}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=103MF {ECO:0000313|EMBL:SFS53054.1,
RC   ECO:0000313|Proteomes:UP000198993};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FPAF01000001; SFS53054.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6QKR6; -.
DR   STRING; 1761751.SAMN04488145_1011056; -.
DR   OrthoDB; 9773088at2; -.
DR   Proteomes; UP000198993; Unassembled WGS sequence.
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          5..218
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   265 AA;  29169 MW;  F4F44BFD8DE23EEE CRC64;
     MGEAIVITSG KGGVGKTTTS ANIGTALALS GKKICLIDTD IGLRNLDVVM GLENRIVYDL
     VDVVEGRCRL PQALIRDKRF DELYLLPAAQ TSDKSAVTPE QMEELIQQLR QDYDYILIDC
     PAGIEQGFKN AVAGADKAIV VTTPEVSSMR DADRIIGLLE KEDIEPPKLI INRVRGHMLH
     EQDMLDVDEI VRTLSIELLG VVEDDDEVIR ATNTGEPVAL QPNGKASIAY RNIARRLLGE
     NVPLQPLENG KESVFTKMKK FFGIR
//
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