MIND_THEMA
ID MIND_THEMA Reviewed; 271 AA.
AC Q9X2I3;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Septum site-determining protein MinD;
DE AltName: Full=Cell division inhibitor MinD;
GN Name=minD; OrderedLocusNames=TM_1870;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36932.1; -; Genomic_DNA.
DR PIR; A72200; A72200.
DR RefSeq; NP_229666.1; NC_000853.1.
DR RefSeq; WP_004082421.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X2I3; -.
DR SMR; Q9X2I3; -.
DR STRING; 243274.THEMA_04820; -.
DR EnsemblBacteria; AAD36932; AAD36932; TM_1870.
DR KEGG; tma:TM1870; -.
DR KEGG; tmw:THMA_1920; -.
DR PATRIC; fig|243274.18.peg.933; -.
DR eggNOG; COG2894; Bacteria.
DR InParanoid; Q9X2I3; -.
DR OMA; CESAKAY; -.
DR OrthoDB; 1631847at2; -.
DR Proteomes; UP000008183; 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 3: Inferred from homology;
KW ATP-binding; Cell cycle; Cell division; Cell membrane; Membrane;
KW Nucleotide-binding; Reference proteome; Septation.
FT CHAIN 1..271
FT /note="Septum site-determining protein MinD"
FT /id="PRO_0000201975"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ SEQUENCE 271 AA; 29483 MW; EC76D3F15D64A4CA CRC64;
MGNVIVVTSG KGGVGKTTIT ANLGCALAKL GEKVCLIDAD IGLKNLDIVL GLENRIVYTM
IDVVNGKVSP QEALVKHKML KNLYLLPASQ IATKEMISPN DMKAIVKELI PHFDYIIIDS
PAGIERGFRN AVAPAERVLV VTTPELPAIS DADRVIGLLE NFGFSDEKIN VIINRFKPHM
VKKGEMLTTD DIKHTLSLEI IAVIPDSEDI IVASNTGIPV SLNGNSRISK NFENLARRIR
GEGVPLENDF VTVSKGLIDT LKDFFSKLKR G
