ID A0A378JKG8_9GAMM Unreviewed; 276 AA.
AC A0A378JKG8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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:STX51826.1};
GN ORFNames=NCTC13316_01925 {ECO:0000313|EMBL:STX51826.1};
OS Legionella busanensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=190655 {ECO:0000313|EMBL:STX51826.1, ECO:0000313|Proteomes:UP000254794};
RN [1] {ECO:0000313|EMBL:STX51826.1, ECO:0000313|Proteomes:UP000254794}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13316 {ECO:0000313|EMBL:STX51826.1,
RC ECO:0000313|Proteomes:UP000254794};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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 -!- 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}.
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DR EMBL; UGOD01000001; STX51826.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378JKG8; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000254794; Unassembled WGS sequence.
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 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; 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:0000313|EMBL:STX51826.1};
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 276 AA; 29846 MW; D598C53EF901550A CRC64;
MAKIIVVTSG KGGVGKTTTS AAISSGLALQ GHKTVVVDFD IGLRNLDIIM GCERRVVFDF
VNVINGEASL NQALIKDKRI PQLCILPASQ TRDKDALTLE GVGKVLTDLS AEFDYIVCDS
PAGIETGALM AMYYADHAIV VTNPEVSSVR DSDRILGILA SKTKRAIEND SPVQEHLLLT
RYDPIRVEKG EMLSVEDVKE ILAIPLIGVV PESKAVLKAS NTGTPVILDE VSDAGLAYKD
AIARFLGESR PMRFISPERK GLLRRLFSKN KEDVPA
//
