ID Q7MML1_VIBVY Unreviewed; 270 AA.
AC Q7MML1;
DT 15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=Septum site-determining protein MinD {ECO:0000256|ARBA:ARBA00016887};
DE AltName: Full=Cell division inhibitor MinD {ECO:0000256|ARBA:ARBA00032845};
GN OrderedLocusNames=VV1056 {ECO:0000313|EMBL:BAC93820.1};
OS Vibrio vulnificus (strain YJ016).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=196600 {ECO:0000313|EMBL:BAC93820.1, ECO:0000313|Proteomes:UP000002675};
RN [1] {ECO:0000313|EMBL:BAC93820.1, ECO:0000313|Proteomes:UP000002675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YJ016 {ECO:0000313|EMBL:BAC93820.1,
RC ECO:0000313|Proteomes:UP000002675};
RX PubMed=14656965; DOI=10.1101/gr.1295503;
RA Chen C.Y., Wu K.M., Chang Y.C., Chang C.H., Tsai H.C., Liao T.L., Liu Y.M.,
RA Chen H.J., Shen A.B., Li J.C., Su T.L., Shao C.P., Lee C.T., Hor L.I.,
RA Tsai S.F.;
RT "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL Genome Res. 13:2577-2587(2003).
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 ---------------------------------------------------------------------------
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; BA000037; BAC93820.1; -; Genomic_DNA.
DR RefSeq; WP_011149811.1; NC_005139.1.
DR AlphaFoldDB; Q7MML1; -.
DR STRING; 672.VV93_v1c09790; -.
DR GeneID; 66964298; -.
DR KEGG; vvy:VV1056; -.
DR PATRIC; fig|196600.6.peg.1053; -.
DR eggNOG; COG2894; Bacteria.
DR HOGENOM; CLU_037612_0_1_6; -.
DR Proteomes; UP000002675; Chromosome I.
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 Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 3..157
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 270 AA; 29420 MW; 4A1BC03B79A7CFD3 CRC64;
MARIIVVTSG KGGVGKTTSS AAIASGLALK GKKTAVIDFD IGLRNLDLIM GCERRVVYDF
VNVINGEATL NQAMIKDKRV DNLFILPASQ TRDKDALTKE GVKRVLDELD EMGFDFVICD
SPAGIEQGAL MALYFADEAI VTTNPEVSSV RDSDRILGIL DSKSLRAEQG LEPVKQHLLL
TRYNPARVNL GEMLSVEDVE EILHISLLGV IPESQAVLNA SNKGVPVIFD ENTDAGMAYS
DTVDRLLGNQ VDFRFLTEEK KGLFKRLFGG
//
