ID A0A2R4C516_9BURK Unreviewed; 271 AA.
AC A0A2R4C516;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-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:AVR94717.1};
GN ORFNames=C9I28_02520 {ECO:0000313|EMBL:AVR94717.1};
OS Pseudoduganella armeniaca.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Pseudoduganella.
OX NCBI_TaxID=2072590 {ECO:0000313|EMBL:AVR94717.1, ECO:0000313|Proteomes:UP000240505};
RN [1] {ECO:0000313|EMBL:AVR94717.1, ECO:0000313|Proteomes:UP000240505}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZMN-3 {ECO:0000313|EMBL:AVR94717.1,
RC ECO:0000313|Proteomes:UP000240505};
RA Huang H., Ren M.;
RT "Massilia armeniaca sp. nov., isolated from desert soil.";
RL Submitted (MAR-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; CP028324; AVR94717.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R4C516; -.
DR KEGG; masz:C9I28_02520; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000240505; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000240505}.
FT DOMAIN 3..163
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 271 AA; 29642 MW; AECC93C94AEC094A CRC64;
MARIIVVTSG KGGVGKTTSS ASFSTGLAMR GHKTVVIDFD VGLRNLDLIM GCERRVVYDL
INVINKEASL HQALIKDKHC DNLFILPASQ TRDKDALSED GVEAVLAELI NMGFEFIICD
SPAGIEHGAL MALTFADEAL IVTNPEVSSV RDSDRILGII QAKSRRAQSG GEPVKEHLLI
TRYSPKRVEA GEMLSYTDVQ EILRIPLIGI IPESEQVLHA SNQGNPAIHF KGTDVAEAYE
DVVARFLGEQ KPLRFTDYEK PGLLKRIFGA K
//
