ID A0A1U7MK98_9FIRM Unreviewed; 263 AA.
AC A0A1U7MK98;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, 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 Name=minD_3 {ECO:0000313|EMBL:OLS57914.1};
GN ORFNames=SPSPH_14480 {ECO:0000313|EMBL:OLS57914.1};
OS Sporomusa sphaeroides DSM 2875.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC Sporomusa.
OX NCBI_TaxID=1337886 {ECO:0000313|EMBL:OLS57914.1, ECO:0000313|Proteomes:UP000186950};
RN [1] {ECO:0000313|EMBL:OLS57914.1, ECO:0000313|Proteomes:UP000186950}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2875 {ECO:0000313|EMBL:OLS57914.1,
RC ECO:0000313|Proteomes:UP000186950};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Sporomusa sphaeroides DSM 2875.";
RL Submitted (FEB-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 -!- 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:OLS57914.1}.
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DR EMBL; LSLJ01000001; OLS57914.1; -; Genomic_DNA.
DR RefSeq; WP_075754608.1; NZ_LSLJ01000001.1.
DR AlphaFoldDB; A0A1U7MK98; -.
DR STRING; 1337886.SPSPH_14480; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000186950; 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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000186950}.
FT DOMAIN 3..161
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 263 AA; 28760 MW; BD2927B473DE576A CRC64;
MGEVIVITSG KGGVGKTTTT ANIGTGFALQ GKKVVLVDAD IGLRNLDVVM GLENRIVYDL
VDVTEGNCRL KQALIRDKRY ETLYLLPAAQ TRDKNAVTPD QMQQLCKDLA QEFDYVIIDC
PAGIEQGFKN AIAGADRAII VTTPEVSAVR DADRIIGLLE SEGKHNPKLI VNRIRPLMVK
KGDMMDIDDI IEILAVDLLG IIPEDEYIVI STNRGEPAVV NNSALASTAY RNIVRRLTGE
NVPLMVLETN ESLWGKFKKV LGL
//
