ID   V1CEA5_9FIRM            Unreviewed;       241 AA.
AC   V1CEA5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
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=HMPREF9089_01166 {ECO:0000313|EMBL:ESE29643.1};
OS   Eubacterium brachy ATCC 33089.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales;
OC   Eubacteriales Family XIII. Incertae Sedis.
OX   NCBI_TaxID=1321814 {ECO:0000313|EMBL:ESE29643.1, ECO:0000313|Proteomes:UP000017536};
RN   [1] {ECO:0000313|EMBL:ESE29643.1, ECO:0000313|Proteomes:UP000017536}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33089 {ECO:0000313|EMBL:ESE29643.1,
RC   ECO:0000313|Proteomes:UP000017536};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) 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:ESE29643.1}.
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DR   EMBL; AXUD01000011; ESE29643.1; -; Genomic_DNA.
DR   AlphaFoldDB; V1CEA5; -.
DR   STRING; 1321814.HMPREF9089_01166; -.
DR   PATRIC; fig|1321814.3.peg.1113; -.
DR   eggNOG; COG2894; Bacteria.
DR   HOGENOM; CLU_037612_0_1_9; -.
DR   OrthoDB; 9773088at2; -.
DR   Proteomes; UP000017536; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:UP000017536}.
FT   DOMAIN          5..218
FT                   /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT                   /evidence="ECO:0000259|Pfam:PF01656"
SQ   SEQUENCE   241 AA;  26812 MW;  3360729342CC634C CRC64;
     MGKTILIASG KGGTGKTMFA ANIGALLAIE GKRVLLVDMD LGLRNLDLYL GLEDKIVYNV
     MDVLSGICSI SKAMVRDRRF ENLFFMAASP CIDDRDITQL HMKVLYEKLK KKFDYIIVDA
     PAGASDGLDV LAVEVDRAVV ITEAENASIR DADVVEKRLR NHGITDIRCI INKVNVELMT
     TGIVPNLDEI MSKLNMVVIG FMQWDENIYI ATNRGVPIVL KDDTYITKNF KKILGRILEN
     S
//