ID G7MAA8_9CLOT Unreviewed; 266 AA.
AC G7MAA8;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
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=CDLVIII_5545 {ECO:0000313|EMBL:EHJ02019.1};
OS Clostridium sp. DL-VIII.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=641107 {ECO:0000313|EMBL:EHJ02019.1, ECO:0000313|Proteomes:UP000005106};
RN [1] {ECO:0000313|EMBL:EHJ02019.1, ECO:0000313|Proteomes:UP000005106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DL-VIII {ECO:0000313|EMBL:EHJ02019.1,
RC ECO:0000313|Proteomes:UP000005106};
RX PubMed=23929491;
RA Taghavi S., Izquierdo J.A., van der Lelie D.;
RT "Complete Genome Sequence of Clostridium sp. Strain DL-VIII, a Novel
RT Solventogenic Clostridium Species Isolated from Anaerobic Sludge.";
RL Genome Announc. 1:e00605-e00613(2013).
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}.
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DR EMBL; CM001240; EHJ02019.1; -; Genomic_DNA.
DR RefSeq; WP_009172657.1; NZ_CM001240.1.
DR AlphaFoldDB; G7MAA8; -.
DR STRING; 641107.CDLVIII_5545; -.
DR eggNOG; COG2894; Bacteria.
DR HOGENOM; CLU_037612_0_1_9; -.
DR Proteomes; UP000005106; Chromosome.
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:UP000005106}.
FT DOMAIN 5..155
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 266 AA; 29081 MW; C2111CC80766D978 CRC64;
MGVSIVVTSG KGGVGKTTTT ANIGTALASL GKKVVVIDGD TGLRNLDVLL GLENRIVYTI
IDVIEGRCRL KQGLIKDKRF QNLCLLPTAQ TKDKDDISPQ EMLKIVNELK EEFDYVLIDS
PAGIEQGFEN AVIGAEKAII VVNPEITSVR DADRVIGKLD AKGLDDHSVI INRLNYEMTK
NGDMLDVSDI IETLSIELLG VVPDDKNITI STNKGEPIVL DENAFAGQAF KNIARRIMGE
EVPLMNLHIE EHQGFLGSLK KLFKRN
//
