ID   MIND_BUCBP              Reviewed;         270 AA.
AC   Q89AI3;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Septum site-determining protein MinD;
DE   AltName: Full=Cell division inhibitor MinD;
GN   Name=minD; OrderedLocusNames=bbp_303;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO27028.1; -; Genomic_DNA.
DR   RefSeq; WP_011091429.1; NC_004545.1.
DR   AlphaFoldDB; Q89AI3; -.
DR   SMR; Q89AI3; -.
DR   STRING; 224915.bbp_303; -.
DR   EnsemblBacteria; AAO27028; AAO27028; bbp_303.
DR   GeneID; 56470843; -.
DR   KEGG; bab:bbp_303; -.
DR   eggNOG; COG2894; Bacteria.
DR   HOGENOM; CLU_037612_0_1_6; -.
DR   OMA; CESAKAY; -.
DR   OrthoDB; 1631847at2; -.
DR   Proteomes; UP000000601; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR   InterPro; IPR010223; MinD.
DR   InterPro; IPR025501; MinD_FleN.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   Pfam; PF01656; CbiA; 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; Reference proteome; 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_0000201967"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   270 AA;  29801 MW;  C18CE20E10D6FDF6 CRC64;
     MTRIIVVTSG KGGVGKTTSS AALATGFAKK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF
     INVINGEAIL NQALIKDKRT EGLFILPASQ TRNKNALTKS GIDRVFTQLV NMNFDIIICD
     SPAGIESGAV LAIYFSDEAI VITNPEVSSV RDSDRILGII ASTSQRSSQN FKPIKEHLLL
     TRYNPKRVSN GDMLSTEDVL DILRIPLIGV IPEDTSVLKA SNQGTPVILN YNSNAGQAYY
     DTVNRLLGIN CPFRFVKDEK KSFLRRLFRR