ID   MIND_BACSU              Reviewed;         268 AA.
AC   Q01464;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1993, sequence version 1.
DT   03-AUG-2022, entry version 143.
DE   RecName: Full=Septum site-determining protein MinD;
DE   AltName: Full=Cell division inhibitor MinD;
GN   Name=minD; Synonyms=divIVB; OrderedLocusNames=BSU27990;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1400225; DOI=10.1128/jb.174.21.6729-6742.1992;
RA   Varley A.W., Stewart G.C.;
RT   "The divIVB region of the Bacillus subtilis chromosome encodes homologs of
RT   Escherichia coli septum placement (minCD) and cell shape (mreBCD)
RT   determinants.";
RL   J. Bacteriol. 174:6729-6742(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8459776; DOI=10.1111/j.1365-2958.1993.tb01151.x;
RA   Lee S., Price C.W.;
RT   "The minCD locus of Bacillus subtilis lacks the minE determinant that
RT   provides topological specificity to cell division.";
RL   Mol. Microbiol. 7:601-610(1993).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1400224; DOI=10.1128/jb.174.21.6717-6728.1992;
RA   Levin P.A., Margolis P.S., Setlow P., Losick R., Sun D.;
RT   "Identification of Bacillus subtilis genes for septum placement and shape
RT   determination.";
RL   J. Bacteriol. 174:6717-6728(1992).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [5]
RP   INTERACTION WITH MINJ.
RC   STRAIN=3610;
RX   PubMed=18976281; DOI=10.1111/j.1365-2958.2008.06469.x;
RA   Patrick J.E., Kearns D.B.;
RT   "MinJ (YvjD) is a topological determinant of cell division in Bacillus
RT   subtilis.";
RL   Mol. Microbiol. 70:1166-1179(2008).
RN   [6]
RP   INTERACTION WITH MINJ.
RC   STRAIN=168;
RX   PubMed=19019154; DOI=10.1111/j.1365-2958.2008.06501.x;
RA   Bramkamp M., Emmins R., Weston L., Donovan C., Daniel R.A., Errington J.;
RT   "A novel component of the division-site selection system of Bacillus
RT   subtilis and a new mode of action for the division inhibitor MinCD.";
RL   Mol. Microbiol. 70:1556-1569(2008).
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 (By similarity). Interacts with
CC       MinJ. {ECO:0000250, ECO:0000269|PubMed:18976281,
CC       ECO:0000269|PubMed:19019154}.
CC   -!- INTERACTION:
CC       Q01464; Q01463: minC; NbExp=3; IntAct=EBI-6502875, EBI-9304968;
CC       Q01464; P96716: ywqD; NbExp=4; IntAct=EBI-6502875, EBI-9302929;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC   -!- SIMILARITY: Belongs to the ParA family. MinD subfamily. {ECO:0000305}.
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DR   EMBL; M95582; AAA22609.1; -; Genomic_DNA.
DR   EMBL; Z15113; CAA78818.1; -; Genomic_DNA.
DR   EMBL; M96343; AAA22401.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14759.1; -; Genomic_DNA.
DR   PIR; S31205; G45239.
DR   RefSeq; NP_390677.1; NC_000964.3.
DR   RefSeq; WP_004398624.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; Q01464; -.
DR   SMR; Q01464; -.
DR   IntAct; Q01464; 8.
DR   MINT; Q01464; -.
DR   STRING; 224308.BSU27990; -.
DR   jPOST; Q01464; -.
DR   PaxDb; Q01464; -.
DR   PRIDE; Q01464; -.
DR   EnsemblBacteria; CAB14759; CAB14759; BSU_27990.
DR   GeneID; 937499; -.
DR   KEGG; bsu:BSU27990; -.
DR   PATRIC; fig|224308.179.peg.3041; -.
DR   eggNOG; COG2894; Bacteria.
DR   InParanoid; Q01464; -.
DR   OMA; CESAKAY; -.
DR   PhylomeDB; Q01464; -.
DR   BioCyc; BSUB:BSU27990-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0009898; C:cytoplasmic side of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central.
DR   GO; GO:0000917; P:division septum assembly; IEA:UniProtKB-KW.
DR   GO; GO:0051782; P:negative regulation of cell division; IBA:GO_Central.
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   1: Evidence at protein level;
KW   ATP-binding; Cell cycle; Cell division; Cell membrane; Membrane;
KW   Nucleotide-binding; Reference proteome; Septation.
FT   CHAIN           1..268
FT                   /note="Septum site-determining protein MinD"
FT                   /id="PRO_0000201964"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   268 AA;  29407 MW;  6665E9F693F58A9B CRC64;
     MGEAIVITSG KGGVGKTTTS ANLGTALAIL GKRVCLVDTD IGLRNLDVVM GLENRIIYDL
     VDVVEGRCKM HQALVKDKRF DDLLYLMPAA QTSDKTAVAP EQIKNMVQEL KQEFDYVIID
     CPAGIEQGYK NAVSGADKAI VVTTPEISAV RDADRIIGLL EQEENIEPPR LVVNRIRNHL
     MKNGDTMDID EIVQHLSIDL LGIVADDDEV IKASNHGEPI AMDPKNRASI AYRNIARRIL
     GESVPLQVLE EQNKGMMAKI KSFFGVRS