ID   A0A1H0WNE2_9BURK        Unreviewed;       271 AA.
AC   A0A1H0WNE2;
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=SAMN05216303_11082 {ECO:0000313|EMBL:SDP92199.1};
OS   Rhodoferax sp. OV413.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Rhodoferax.
OX   NCBI_TaxID=1855285 {ECO:0000313|EMBL:SDP92199.1, ECO:0000313|Proteomes:UP000199151};
RN   [1] {ECO:0000313|Proteomes:UP000199151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV413 {ECO:0000313|Proteomes:UP000199151};
RA   Varghese N., Submissions S.;
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   -!- 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; FNJA01000010; SDP92199.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H0WNE2; -.
DR   STRING; 1855285.SAMN05216303_11082; -.
DR   OrthoDB; 9773088at2; -.
DR   Proteomes; UP000199151; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199151}.
FT   DOMAIN          5..226
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   271 AA;  29569 MW;  DCD8CBBB935892DA CRC64;
     MSKIIVVTSG KGGVGKTTTS ASFASGLALR GHKTAVIDFD VGLRNLDLIM GCERRVVYDL
     INVIHNEANL NQALIKDKQC DNLFVLAASQ TRDKDALTQD GVERVLKDLG EMGFEYIVCD
     SPAGIETGAL MAMHFADDAL VVTNPEVSSV RDSDRILGML GSKTKRAIEG LAPVKEHLVI
     TRYNPTRVED GHMLSLEDIQ DILRIPLMGV IPESETVLQA SNQGLPAIHL NETDVSEAYK
     DVVARFLGEE KPMRFVDAVK PGFFKRLFGG K
//