ID S0EWA6_CHTCT Unreviewed; 271 AA.
AC S0EWA6;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=CCALI_02279 {ECO:0000313|EMBL:CCW36086.1};
OS Chthonomonas calidirosea (strain DSM 23976 / ICMP 18418 / T49).
OC Bacteria; Armatimonadota; Chthonomonadetes; Chthonomonadales;
OC Chthonomonadaceae; Chthonomonas.
OX NCBI_TaxID=1303518 {ECO:0000313|EMBL:CCW36086.1, ECO:0000313|Proteomes:UP000014227};
RN [1] {ECO:0000313|Proteomes:UP000014227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23976 / ICMP 18418 / T49
RC {ECO:0000313|Proteomes:UP000014227};
RA Lee K.C.Y., Morgan X.C., Dunfield P.F., Tamas I., Houghton K.M.,
RA Vyssotski M., Ryan J.L.J., Lagutin K., McDonald I.R., Stott M.B.;
RT "Genome sequence of Chthonomonas calidirosea, the first sequenced genome
RT from the Armatimonadetes phylum (formally candidate division OP10).";
RL Submitted (MAR-2013) 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 -!- SIMILARITY: Belongs to the ParA family. MinD subfamily.
CC {ECO:0000256|ARBA:ARBA00010257}.
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DR EMBL; HF951689; CCW36086.1; -; Genomic_DNA.
DR RefSeq; WP_016483606.1; NC_021487.1.
DR AlphaFoldDB; S0EWA6; -.
DR STRING; 454171.CP488_01816; -.
DR KEGG; ccz:CCALI_02279; -.
DR PATRIC; fig|1303518.3.peg.2369; -.
DR eggNOG; COG2894; Bacteria.
DR HOGENOM; CLU_037612_0_1_0; -.
DR InParanoid; S0EWA6; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000014227; Chromosome.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000014227}.
FT DOMAIN 8..223
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 271 AA; 29527 MW; E5F01577499ADAB9 CRC64;
MTCEARVIVI TSGKGGVGKT TTTANIGVAL AALGDKVALV DADIGLRNLD LALGLENRIV
YDIVDVVEGR AKLRQALVRD KRHQNLVLLP AAQTRDKSAV SPRQMQQVIT ELKDEGFGFI
LIDCPAGIEQ GFRNATAGAT EAIVVTNPEM ASVRDADRII GLLEAQELRD PMLVVNRIRV
QMVKNQEMLG VEDVQEVLGK SVRLLGIVPD DESIITSTNR GEPAVLSENS LAGRAFHNIA
RRLRGEEVPF SELEEKTGLL ERLRKMFAGK R
//
