ID A0A2N7UJ07_9GAMM Unreviewed; 272 AA.
AC A0A2N7UJ07;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:PMR80385.1};
GN ORFNames=C1H70_09325 {ECO:0000313|EMBL:PMR80385.1};
OS Halomonas urumqiensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1684789 {ECO:0000313|EMBL:PMR80385.1, ECO:0000313|Proteomes:UP000235547};
RN [1] {ECO:0000313|EMBL:PMR80385.1, ECO:0000313|Proteomes:UP000235547}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BZ-SZ-XJ27 {ECO:0000313|EMBL:PMR80385.1,
RC ECO:0000313|Proteomes:UP000235547};
RA Chen C.;
RT "Halomonas endophytica sp. nov., isolated from storage liquid in the stems
RT of Populus euphratica.";
RL Submitted (JAN-2018) 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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004202};
CC Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004202}.
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:PMR80385.1}.
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DR EMBL; PNRG01000018; PMR80385.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7UJ07; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000235547; Unassembled WGS sequence.
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 CDD; cd02036; MinD; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_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; PF13614; AAA_31; 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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000235547};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 3..156
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 272 AA; 29568 MW; 97C873CCD7B11013 CRC64;
MAKIIVVTSG KGGVGKTTSA AAIATGLALR GNKTVVIDFD VGLRNLDLIM GCERRVVYDL
VNVIQGEAGL NQALIRDKRV DNLHILPASQ TRDKDALSVE GVEKVLETLS KDFDFIICDS
PAGIERGAQL AMYFADAAIV VTNPEVSSVR DSDRMLGLLA SKTRRAERGD DPIQEHLLIT
RYNPSRVDLG DMLNLEDIRE ILAIDLIGLI PESEAVLRAS NQGVPVTHDA TSDAGQAYTD
TVARLLGEDV PLRFHEYQKK SLLSRMFGGG RR
//
