ID A0A1L6HZI8_9BURK Unreviewed; 271 AA.
AC A0A1L6HZI8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BTO02_16220 {ECO:0000313|EMBL:APR36695.1};
OS Paraburkholderia sp. SOS3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR36695.1, ECO:0000313|Proteomes:UP000184708};
RN [1] {ECO:0000313|EMBL:APR36695.1, ECO:0000313|Proteomes:UP000184708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SOS3 {ECO:0000313|EMBL:APR36695.1,
RC ECO:0000313|Proteomes:UP000184708};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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; CP018811; APR36695.1; -; Genomic_DNA.
DR RefSeq; WP_075157893.1; NZ_CP018811.1.
DR AlphaFoldDB; A0A1L6HZI8; -.
DR STRING; 1926494.BTO02_16220; -.
DR KEGG; para:BTO02_16220; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000184708; Chromosome 1.
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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 3..157
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 271 AA; 29652 MW; 8C899B4A4D3BD8B6 CRC64;
MAKIIVVTSG KGGVGKTTTS ASFSSGLALR GHKTAVIDFD VGLRNLDLIM GCERRVVYDL
INVIQGEANL NQALIKDKKL ENLYILPASQ TRDKDALTME GVEKVINDLV AMDFEYIVCD
SPAGIESGAL LAMHFADEAL IVTNPEVSSV RDSDRILGIL SSKTKRAIEG KEPIKEHLLI
TRYNPKRVSE GEMLSLSDIQ EILRIDLIGV IPESEAVLHA SNQGLPAVHL DGTDVAESYK
DVVSRFLGEQ KSLRFTDYQK PGLLQRLFGT K
//
