ID   MIND_ECOL6              Reviewed;         270 AA.
AC   P0AEZ4; P18197;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Septum site-determining protein MinD;
DE   AltName: Full=Cell division inhibitor MinD;
GN   Name=minD; OrderedLocusNames=c1622;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(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 inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. {ECO:0000305}.
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DR   EMBL; AE014075; AAN80087.1; -; Genomic_DNA.
DR   RefSeq; WP_000101055.1; NC_004431.1.
DR   AlphaFoldDB; P0AEZ4; -.
DR   SMR; P0AEZ4; -.
DR   STRING; 199310.c1622; -.
DR   EnsemblBacteria; AAN80087; AAN80087; c1622.
DR   GeneID; 66675005; -.
DR   KEGG; ecc:c1622; -.
DR   eggNOG; COG2894; Bacteria.
DR   HOGENOM; CLU_037612_0_1_6; -.
DR   OMA; CESAKAY; -.
DR   BioCyc; ECOL199310:C1622-MON; -.
DR   Proteomes; UP000001410; 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 inner membrane; Cell membrane;
KW   Membrane; 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_0000201970"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   270 AA;  29614 MW;  0D2C4C0976B77D2C CRC64;
     MARIIVVTSG KGGVGKTTSS AAIATGLAQK GKKTVVIDFD IGLRNLDLIM GCERRVVYDF
     VNVIQGDATL NQALIKDKRT ENLYILPASQ TRDKDALTRE GVAKVLDDLK AMDFEFIVCD
     SPAGIETGAL MALYFADEAI ITTNPEVSSV RDSDRILGIL ASKSRRAENG EEPIKEHLLL
     TRYNPGRVSR GDMLSMEDVL EILRIKLVGV IPEDQSVLRA SNQGEPVILD INADAGKAYA
     DTVERLLGEE RPFRFIEEEK KGFLKRLFGG