ID C0D9Y0_9FIRM Unreviewed; 263 AA.
AC C0D9Y0;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:EEG51855.1};
GN ORFNames=CLOSTASPAR_06080 {ECO:0000313|EMBL:EEG51855.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG51855.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG51855.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51855.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG51855.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51855.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) 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:EEG51855.1}.
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DR EMBL; ACCJ01000514; EEG51855.1; -; Genomic_DNA.
DR RefSeq; WP_007718407.1; NZ_GG657592.1.
DR AlphaFoldDB; C0D9Y0; -.
DR HOGENOM; CLU_037612_0_1_9; -.
DR Proteomes; UP000004756; 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}.
FT DOMAIN 3..161
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 263 AA; 28647 MW; C81FA11C8632BE4F CRC64;
MSEVIVITSG KGGVGKTTTS ANVGTGLAIL GKRVVLIDTD IGLRNLDVVM GLENRIVYNL
VDVVEGNCRM KQALIRDKRY PNLYLLPSAQ TRDKTSVTPE QMVKLVDDLR SDFDYILLDC
PAGIEQGFRN AIAGADRALV VTTPEVSAIR DADRIIGLLE HAEMEEIDLI VNRIRMDMVR
RGDMMSLSDV SDILAVNIIG AVPDDENIVV STNQGEPLVG MGSQSGSAYL DICRRILGEN
IPVVGPEQPK RFLARLCGIL KRA
//
