ID   MIND_HELPJ              Reviewed;         268 AA.
AC   Q9ZMA8;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-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=jhp_0314;
OS   Helicobacter pylori (strain J99 / ATCC 700824) (Campylobacter pylori J99).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J99 / ATCC 700824;
RX   PubMed=9923682; DOI=10.1038/16495;
RA   Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C.,
RA   Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J.,
RA   Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D.,
RA   Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.;
RT   "Genomic sequence comparison of two unrelated isolates of the human gastric
RT   pathogen Helicobacter pylori.";
RL   Nature 397:176-180(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; AE001439; AAD05905.1; -; Genomic_DNA.
DR   PIR; B71945; B71945.
DR   RefSeq; WP_001019064.1; NZ_CP011330.1.
DR   AlphaFoldDB; Q9ZMA8; -.
DR   SMR; Q9ZMA8; -.
DR   STRING; 85963.jhp_0314; -.
DR   PRIDE; Q9ZMA8; -.
DR   EnsemblBacteria; AAD05905; AAD05905; jhp_0314.
DR   KEGG; hpj:jhp_0314; -.
DR   PATRIC; fig|85963.30.peg.699; -.
DR   eggNOG; COG2894; Bacteria.
DR   OMA; CESAKAY; -.
DR   Proteomes; UP000000804; 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; Septation.
FT   CHAIN           1..268
FT                   /note="Septum site-determining protein MinD"
FT                   /id="PRO_0000201972"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q72H90"
SQ   SEQUENCE   268 AA;  29265 MW;  1F479C187A201A63 CRC64;
     MAIVVTITSG KGGVGKSTTT ANLAIGLAES GKKVVAVDFD IGLRNLDMIL GLENRIVYDV
     VDVMEKNCNL SQALITDKKT KNLSFLAASQ SKDKNILDKE KVAILINALR ADFDYILIDS
     PAGIESGFEH AILHADMALV VVTPEVSSLR DSDRVIGIID AKSNRAKSGE EVHKHLIINR
     LKPELVANGE MISIEEVLKI LCLPLIGIIP EDHHIISATN KGEPVIRTDC ESAKAYQRIT
     RRILGEEVEY VEFKAKRGFF SALKGIFS