ID A0A2M8GVP0_9VIBR Unreviewed; 270 AA.
AC A0A2M8GVP0;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:PJC85411.1};
GN ORFNames=CSW98_14565 {ECO:0000313|EMBL:PJC85411.1};
OS Vibrio sp. HA2012.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1971595 {ECO:0000313|EMBL:PJC85411.1, ECO:0000313|Proteomes:UP000232179};
RN [1] {ECO:0000313|EMBL:PJC85411.1, ECO:0000313|Proteomes:UP000232179}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HA2012 {ECO:0000313|EMBL:PJC85411.1,
RC ECO:0000313|Proteomes:UP000232179};
RA Wang K.;
RT "The draft genome sequence of Vibrio sediminis HA2012.";
RL Submitted (NOV-2017) 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 -!- 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:PJC85411.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PFXK01000008; PJC85411.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M8GVP0; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000232179; 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; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_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; PF01656; CbiA; 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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000232179};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 5..227
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 270 AA; 29607 MW; A1CD561346AC60EB CRC64;
MARIIVVTSG KGGVGKTTSS AAIASGLALK GKKTAVIDFD IGLRNLDLIM GCERRVVYDF
VNVINGEATL NQALIKDKRA DNLFILPASQ TRDKDALTRD GVQRVFDELD EMGFEFIICD
SPAGIEQGAL MALYFADEAI VTTNPEVSSV RDSDRILGIL DSKSRRAEQG LEPIRQHLLL
TRYNPSRVNL GEMLSVSDVE EILHIKLLGV IPESQAVLNA SNKGVPVIFD EQSDAGQAYD
DTVERLLGEE ADFRFLTEEK KSLFKRLFGG
//