ID Z9JK03_9GAMM Unreviewed; 269 AA.
AC Z9JK03;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=AF72_04055 {ECO:0000313|EMBL:EWS78750.1};
OS Xylella taiwanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=1444770 {ECO:0000313|EMBL:EWS78750.1, ECO:0000313|Proteomes:UP000020406};
RN [1] {ECO:0000313|EMBL:EWS78750.1, ECO:0000313|Proteomes:UP000020406}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PLS229 {ECO:0000313|EMBL:EWS78750.1,
RC ECO:0000313|Proteomes:UP000020406};
RX PubMed=24652975;
RA Su C.C., Deng W.L., Jan F.J., Chang C.J., Huang H., Chen J.;
RT "Draft Genome Sequence of Xylella fastidiosa Pear Leaf Scorch Strain in
RT Taiwan.";
RL Genome Announc. 2:e00166-14(2014).
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:EWS78750.1}.
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DR EMBL; JDSQ01000005; EWS78750.1; -; Genomic_DNA.
DR RefSeq; WP_038270657.1; NZ_VOSE01000002.1.
DR AlphaFoldDB; Z9JK03; -.
DR STRING; 1444770.AF72_04055; -.
DR GeneID; 69682494; -.
DR PATRIC; fig|1444770.3.peg.985; -.
DR eggNOG; COG2894; Bacteria.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000020406; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
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:0000313|EMBL:EWS78750.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Septation {ECO:0000256|ARBA:ARBA00023210}.
FT DOMAIN 5..226
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 269 AA; 28949 MW; C41C3DD420EF4511 CRC64;
MAEIIVITSG KGGVGKTTTS ASLACGLARR GKKVAAIDFD VGLRNLDLIM GCERRVVYDF
VNVIHGEATL KQALIKDKRF DNLYVLAASQ TRDKDALTKE GVEKVLKDLD AEGFDFIFCD
SPAGIEKGAY LAMYFADRAV VVVNPEVSSV RDSDRIIGLL DSKTKKAETG SSVVTTLLLT
RYSPTRVESG EMLSITDVEE VLGLKAIGVI PESGDVLNAS NKGEPVILDN DSSAGLAYED
AVGRILGEDH PMRFTTVEKK SFFSKLFGG
//
