ID A0A167GTG6_9GAMM Unreviewed; 270 AA.
AC A0A167GTG6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN ORFNames=I596_1527 {ECO:0000313|EMBL:ANB17552.1};
OS Dokdonella koreensis DS-123.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dokdonella.
OX NCBI_TaxID=1300342 {ECO:0000313|EMBL:ANB17552.1, ECO:0000313|Proteomes:UP000076830};
RN [1] {ECO:0000313|EMBL:ANB17552.1, ECO:0000313|Proteomes:UP000076830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-123 {ECO:0000313|EMBL:ANB17552.1,
RC ECO:0000313|Proteomes:UP000076830};
RA Kim J.F., Lee H., Kwak M.-J.;
RT "Complete genome sequence of Dokdonella koreensis DS-123T.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- SUBUNIT: Interacts with MinC and FtsZ. {ECO:0000256|ARBA:ARBA00011626}.
CC -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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DR EMBL; CP015249; ANB17552.1; -; Genomic_DNA.
DR RefSeq; WP_067645840.1; NZ_CP015249.1.
DR AlphaFoldDB; A0A167GTG6; -.
DR STRING; 1300342.I596_1527; -.
DR KEGG; dko:I596_1527; -.
DR PATRIC; fig|1300342.3.peg.1488; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000076830; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom.
DR InterPro; IPR010223; MinD.
DR InterPro; IPR025501; MinD_FleN.
DR InterPro; IPR027417; P-loop_NTPase.
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; PF01656; CbiA; 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 Cell cycle {ECO:0000256|ARBA:ARBA00023210};
KW Cell division {ECO:0000256|ARBA:ARBA00023210};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000076830};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 5..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 270 AA; 29159 MW; A8F167F0898D2812 CRC64;
MTEFIVVTSG KGGVGKTTSS ASLAVGLARR GKKVAVIDFD VGLRNLDLIM GCERRVVYDF
VNVIHGECTL KQALIKDKRF DSLYVLAASQ TRDKEALTKD GVERVLKELA DEGFDYVICD
SPAGIEKGAA LAMYFADRAV VVVNPEVSSV RDSDRILGLL SSKTRRAELG NGGVEQHLLL
TRYNPARVEA GDMMSIKDVQ EILGIEVLGV IPESEGVLAA SNAGVPVILD DQSYAGQAYD
DAVARLLGEQ RSMRFLDAQK KGLFARIFGS
//
