ID A0A0D8ZV81_9CYAN Unreviewed; 268 AA.
AC A0A0D8ZV81;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
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=UH38_05910 {ECO:0000313|EMBL:KJH72650.1};
OS Aliterella atlantica CENA595.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Chroococcidiopsidales;
OC Aliterellaceae; Aliterella.
OX NCBI_TaxID=1618023 {ECO:0000313|EMBL:KJH72650.1, ECO:0000313|Proteomes:UP000032452};
RN [1] {ECO:0000313|EMBL:KJH72650.1, ECO:0000313|Proteomes:UP000032452}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CENA595 {ECO:0000313|EMBL:KJH72650.1,
RC ECO:0000313|Proteomes:UP000032452};
RA Rigonato J., Alvarenga D.O., Branco L.H., Varani A.M., Brandini F.P.,
RA Fiore M.F.;
RT "Draft genome of a novel marine cyanobacterium (Chroococcales) isolated
RT from South Atlantic Ocean.";
RL Submitted (FEB-2015) 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 -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KJH72650.1}.
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DR EMBL; JYON01000004; KJH72650.1; -; Genomic_DNA.
DR RefSeq; WP_045053711.1; NZ_JYON01000004.1.
DR AlphaFoldDB; A0A0D8ZV81; -.
DR STRING; 1618023.UH38_05910; -.
DR PATRIC; fig|1618023.3.peg.2334; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000032452; Unassembled WGS sequence.
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:UP000032452}.
SQ SEQUENCE 268 AA; 29193 MW; 4FB12511A63D7C7E CRC64;
MSRIIVTTSG KGGVGKTTVT ANLGMALARL GQQVALLDAD FGLRNLDLLL GLENRIVYTA
IEVFAGECRL EQALVKDKRI PGLALLPAAQ NRTKEAVSPE QMTELVDSLI KTFDYVLIDS
PAGIEMGFKN AIAPAKEALI VTTPEISAVR DADRVVGLLE AQGIKRINLI VNRLRPAMVQ
VNDMMSVQDV QEILAIPLIG VVPEDERVIV STNRGEPLVL AETPSMAGMA FDNIARRLQG
ETVEFIDLSV PPENIFSRIR KLLWTKII
//
