ID C0QR63_PERMH Unreviewed; 270 AA.
AC C0QR63;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN Name=minD {ECO:0000313|EMBL:ACO04914.1};
GN OrderedLocusNames=PERMA_1391 {ECO:0000313|EMBL:ACO04914.1};
OS Persephonella marina (strain DSM 14350 / EX-H1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC Persephonella.
OX NCBI_TaxID=123214 {ECO:0000313|EMBL:ACO04914.1, ECO:0000313|Proteomes:UP000001366};
RN [1] {ECO:0000313|EMBL:ACO04914.1, ECO:0000313|Proteomes:UP000001366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14350 / EX-H1 {ECO:0000313|Proteomes:UP000001366};
RX PubMed=19136599; DOI=10.1128/JB.01645-08;
RA Reysenbach A.L., Hamamura N., Podar M., Griffiths E., Ferreira S.,
RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A.,
RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.;
RT "Complete and draft genome sequences of six members of the Aquificales.";
RL J. Bacteriol. 191:1992-1993(2009).
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.
CC {ECO:0000256|ARBA:ARBA00025436}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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DR EMBL; CP001230; ACO04914.1; -; Genomic_DNA.
DR AlphaFoldDB; C0QR63; -.
DR STRING; 123214.PERMA_1391; -.
DR PaxDb; 123214-PERMA_1391; -.
DR KEGG; pmx:PERMA_1391; -.
DR eggNOG; COG2894; Bacteria.
DR HOGENOM; CLU_037612_0_1_0; -.
DR Proteomes; UP000001366; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02036; MinD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033756; YlxH/NBP35.
DR NCBIfam; TIGR01968; minD_bact; 1.
DR PANTHER; PTHR43384:SF6; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC; 1.
DR PANTHER; PTHR43384; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR Pfam; PF10609; ParA; 1.
DR PIRSF; PIRSF003092; MinD; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000001366}.
SQ SEQUENCE 270 AA; 29815 MW; 4D9AF97496504595 CRC64;
MMEERKNGKN ARVFVVTSGK GGVGKTTVTA NVATSLAKMG KKVLTIDADI GLRNLDMILG
LENRIVYDIV DVVEGRVSPE KAFVKDKRGL SLYLLPAAQT KDKEAVKPEQ LVEIIEAVRE
QFDYIFIDSP AGIEGGFKTA AAPADEALVV TNPEVSSVRD ADRIIGLLES MEKENIRLIV
NRIRVHQVKK GEMLSVEDIE EILHIPKVGI VPDEEKMVDF TNKGEPIVLY AENSPAGRAL
INIARRLEGF DVPFDELEVK KGFLSRLFGR
//
