ID A0A0E3Z1T9_9GAMM Unreviewed; 269 AA.
AC A0A0E3Z1T9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=WQ53_02760 {ECO:0000313|EMBL:AKC85842.1};
OS Pseudoxanthomonas suwonensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Pseudoxanthomonas.
OX NCBI_TaxID=314722 {ECO:0000313|EMBL:AKC85842.1, ECO:0000313|Proteomes:UP000033067};
RN [1] {ECO:0000313|EMBL:AKC85842.1, ECO:0000313|Proteomes:UP000033067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J1 {ECO:0000313|EMBL:AKC85842.1,
RC ECO:0000313|Proteomes:UP000033067};
RX PubMed=26067962;
RA Hou L., Jiang J., Xu Z., Zhou Y., Leung F.C.;
RT "Complete Genome Sequence of Pseudoxanthomonas suwonensis Strain J1, a
RT Cellulose-Degrading Bacterium Isolated from Leaf- and Wood-Enriched Soil.";
RL Genome Announc. 3:e00614-15(2015).
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 -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000256|ARBA:ARBA00011626}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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DR EMBL; CP011144; AKC85842.1; -; Genomic_DNA.
DR RefSeq; WP_052630188.1; NZ_CP011144.1.
DR AlphaFoldDB; A0A0E3Z1T9; -.
DR KEGG; psuw:WQ53_02760; -.
DR PATRIC; fig|314722.6.peg.575; -.
DR eggNOG; COG2894; Bacteria.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000033067; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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 Cell cycle {ECO:0000256|ARBA:ARBA00023210};
KW Cell division {ECO:0000313|EMBL:AKC85842.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033067};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 5..226
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 269 AA; 28793 MW; BFD72574E1073DCB CRC64;
MAEIIVVTSG KGGVGKTTSS ASIAIGLAKR GHKTAVIDFD VGLRNLDLIM GCERRVVYDF
VNVVHGEATL KQALIKDKRF DNLYVLAASQ TRDKDALTKE GVEKVLKDLA ADGFDYIVCD
SPAGIEKGAF LAMYFADKAV VVVNPEVSSV RDSDRIIGLL DSKTRKAEAG EAVPSHLLLT
RYSPARVASG EMLSIADVEE VLGLKALGVI PESSDVLNAS NKGEPVILES ESEAGQAYDD
AVGRLLGEER PLRFTTLEKK GFFSKLFGG
//
