ID   A0A1Y2T6V8_SYMTR        Unreviewed;       268 AA.
AC   A0A1Y2T6V8;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=A6D92_06940 {ECO:0000313|EMBL:OTA41417.1};
OS   Symbiobacterium thermophilum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Symbiobacteriaceae;
OC   Symbiobacterium.
OX   NCBI_TaxID=2734 {ECO:0000313|EMBL:OTA41417.1, ECO:0000313|Proteomes:UP000194267};
RN   [1] {ECO:0000313|Proteomes:UP000194267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Antunes L.P., Martins L.F., Pereira R.V., Thomas A.M., Barbosa D.,
RA   Nascimento L., Silva G.M., Condomitti G.W., Digiampietri L.A.,
RA   Lombardi K.C., Ramos P.L., Quaggio R.B., Oliveira J.C., Pascon R.C.,
RA   Cruz J.B., Silva A.M., Setubal J.C.;
RL   Submitted (APR-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   -!- 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:OTA41417.1}.
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DR   EMBL; LWLV01000490; OTA41417.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y2T6V8; -.
DR   Proteomes; UP000194267; 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..219
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   268 AA;  29269 MW;  4F7EFDC11824651C CRC64;
     MGQVIVVTSG KGGVGKTTTT ANLGTALAQL GNRVVLVDAD IGLRNLDVVM GLENRIVYDL
     VDVVEGNARL KQALIKDKRN ENLYLLAAAQ TREKKDVTAE QMRDLTEQLA REFDFVLVDC
     PAGIEDGFKN AIAGAQKAII VANPEVSSVR DADRVIGLWD AQDGDRSPAM LIVNRVRPRM
     VARGDMLEID DMLEMLAVDL LGVVPEDDHI IVSTNRGEPA VYSRDSKAGK AFQNIARRLM
     GEAVPIMDLE AEESLWSRFK RIVGLGRS
//