ID   MIND_BUCAP              Reviewed;         270 AA.
AC   Q8K9L7;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Septum site-determining protein MinD;
DE   AltName: Full=Cell division inhibitor MinD;
GN   Name=minD; OrderedLocusNames=BUsg_317;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67871.1; -; Genomic_DNA.
DR   RefSeq; WP_011053838.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9L7; -.
DR   SMR; Q8K9L7; -.
DR   STRING; 198804.BUsg_317; -.
DR   PRIDE; Q8K9L7; -.
DR   EnsemblBacteria; AAM67871; AAM67871; BUsg_317.
DR   KEGG; bas:BUsg_317; -.
DR   eggNOG; COG2894; Bacteria.
DR   HOGENOM; CLU_037612_0_1_6; -.
DR   OMA; CESAKAY; -.
DR   OrthoDB; 1631847at2; -.
DR   Proteomes; UP000000416; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR025669; AAA_dom.
DR   InterPro; IPR010223; MinD.
DR   InterPro; IPR025501; MinD_FleN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF13614; AAA_31; 1.
DR   PIRSF; PIRSF003092; MinD; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   TIGRFAMs; TIGR01968; minD_bact; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cell cycle; Cell division; Cell membrane; Membrane;
KW   Nucleotide-binding; Septation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..270
FT                   /note="Septum site-determining protein MinD"
FT                   /id="PRO_0000201966"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   270 AA;  30019 MW;  5ACD84EABA99A653 CRC64;
     MTRIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF
     INVIQGDARI QQALIKDKKT KNLFILPASQ TRDKESLTYS GVEKVLNQLI NMEFDFIICD
     SPAGIETGAI LAIYFADEAI VTTNPEVSSV RDSDRILGII SSKSKRSEKN ITPIKEYLLL
     TRYNPTRVKK GEMLSMKDVI EILRIPIIGV IPEDASVLRA SNQGESIILD QNSNAGSAYF
     DTVNRLLGEN HKFRFIEEEK KSFLRRLFGR