ID   MIND_BUCAI              Reviewed;         270 AA.
AC   P57411;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 119.
DE   RecName: Full=Septum site-determining protein MinD;
DE   AltName: Full=Cell division inhibitor MinD;
GN   Name=minD; OrderedLocusNames=BU326;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(2000).
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; BA000003; BAB13034.1; -; Genomic_DNA.
DR   RefSeq; NP_240148.1; NC_002528.1.
DR   RefSeq; WP_010896069.1; NC_002528.1.
DR   AlphaFoldDB; P57411; -.
DR   SMR; P57411; -.
DR   STRING; 107806.10039000; -.
DR   EnsemblBacteria; BAB13034; BAB13034; BAB13034.
DR   KEGG; buc:BU326; -.
DR   PATRIC; fig|107806.10.peg.338; -.
DR   eggNOG; COG2894; Bacteria.
DR   HOGENOM; CLU_037612_0_1_6; -.
DR   OMA; CESAKAY; -.
DR   Proteomes; UP000001806; 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; 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_0000201965"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   270 AA;  29937 MW;  4FCA32C9548A66BA CRC64;
     MTRIIVVTSG KGGVGKTTSS AAIGTGLAQK GKKTIVIDFD IGLRNLDLIM GCERRVVYDF
     INVIQGDATL NQAIIKDKKT NNLFILPASQ TRDKDALTRI GVEKVLTELI KMNFDFIICD
     SPAGIETGAI LAIYFADEAI ITTNPEVSSV RDSDRILGII SSKSKRAEKN ITPIKEYLLL
     TRYNPRRVKK GEMLSMTDVL DILQIPIIGV IPEDQSVLRA SNQGESIILD INSNAGCAYS
     DTVNRLLGEE RHFRFIEEEK KSFLRRLFGR