ID   A0A0C2QPQ0_9CYAN        Unreviewed;       268 AA.
AC   A0A0C2QPQ0;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=SD80_23430 {ECO:0000313|EMBL:KIJ81973.1};
OS   Scytonema tolypothrichoides VB-61278.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Scytonemataceae;
OC   Scytonema.
OX   NCBI_TaxID=1233231 {ECO:0000313|EMBL:KIJ81973.1};
RN   [1] {ECO:0000313|EMBL:KIJ81973.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VB-61278 {ECO:0000313|EMBL:KIJ81973.1};
RA   Tripathy S., Das A., Panda A., Malar M.C., Adhikary S.P.;
RT   "Draft genome sequence of Scytonema tolypothrichoides VB-61278.";
RL   Submitted (JAN-2015) 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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIJ81973.1}.
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; JXCA01000012; KIJ81973.1; -; Genomic_DNA.
DR   STRING; 1233231.SD80_23430; -.
DR   OrthoDB; 9773088at2; -.
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}.
SQ   SEQUENCE   268 AA;  29460 MW;  1E8EF074E94AC931 CRC64;
     MTRIIVTTSG KGGVGKTTIT ANLGMALAKM GRQVALVDAD FGLRNLDLLL GLENRIVYTA
     VEVLARECRL EQALVKDKRQ PNLVLLPAAQ NRTKDAVTPD QMKLLVNALA QKYQYVLVDS
     PAGIEMGFKN AIAPAKEALI ITTPEIASVR DADRVVGLLE AQGIKRIHLI INRIRPAMVR
     ANDMMSVQDV QELLAIPLIG VVPDDERVIV STNRGEPLVL AENPSLAATA FDNIVRRLEG
     ETVEFLELDS TQDNIFSRLR KLFWTKSI
//