ID A0A0R2FNU6_9LACO Unreviewed; 266 AA.
AC A0A0R2FNU6;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=IV38_GL000233 {ECO:0000313|EMBL:KRN29350.1}, IV40_GL000436
GN {ECO:0000313|EMBL:KRN34121.1};
OS Lactobacillus selangorensis.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=81857 {ECO:0000313|EMBL:KRN29350.1, ECO:0000313|Proteomes:UP000051751};
RN [1] {ECO:0000313|Proteomes:UP000051645, ECO:0000313|Proteomes:UP000051751}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-66 {ECO:0000313|EMBL:KRN29350.1,
RC ECO:0000313|Proteomes:UP000051751}, and DSM 13344
RC {ECO:0000313|EMBL:KRN34121.1, ECO:0000313|Proteomes:UP000051645};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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}.
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:KRN29350.1}.
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DR EMBL; JQAT01000001; KRN29350.1; -; Genomic_DNA.
DR EMBL; JQAZ01000001; KRN34121.1; -; Genomic_DNA.
DR RefSeq; WP_057768714.1; NZ_JQAZ01000001.1.
DR AlphaFoldDB; A0A0R2FNU6; -.
DR STRING; 81857.IV38_GL000233; -.
DR PATRIC; fig|81857.3.peg.239; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000051645; Unassembled WGS sequence.
DR Proteomes; UP000051751; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; SEPTUM SITE-DETERMINING PROTEIN MIND HOMOLOG, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR43384:SF6; 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:UP000051645}.
FT DOMAIN 5..220
FT /note="CobQ/CobB/MinD/ParA nucleotide binding"
FT /evidence="ECO:0000259|Pfam:PF01656"
SQ SEQUENCE 266 AA; 29177 MW; 0DF57F8B501D7192 CRC64;
MGTSIVVTSG KGGVGKTTST ANIGTALALL DKKVCLVDLD IGLRNLDVVL GLGNRIIYDI
VDVANGRARI NQALIKDKRF EDNLYLLPAA QNTDKDALTP EQVTQIVDEL RPDFDFILLD
CPAGIEQGFK NAVAGADGAI VVTTPEISAV SDADRVVGLL EEREMKIAPR LVINRIKKHM
MNDGDTMDVD EITKHLSVDL LGIVFDDDAV IRMSNKGQPV ALDPKDNASK CYRNIARRLL
GESVPLMTLK EAKPSFWQRL FHRNRK
//