ID A0A0J0YQ91_9NEIS Unreviewed; 270 AA.
AC A0A0J0YQ91;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=PL75_09080 {ECO:0000313|EMBL:KLT72300.1};
OS Neisseria arctica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT72300.1, ECO:0000313|Proteomes:UP000036027};
RN [1] {ECO:0000313|EMBL:KLT72300.1, ECO:0000313|Proteomes:UP000036027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT72300.1,
RC ECO:0000313|Proteomes:UP000036027};
RA Hansen C.M., Hueffer K., Choi S.C.;
RT "Genome of a novel goose pathogen.";
RL Submitted (NOV-2014) 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}.
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:KLT72300.1}.
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DR EMBL; JTDO01000015; KLT72300.1; -; Genomic_DNA.
DR RefSeq; WP_047761613.1; NZ_JTDO01000015.1.
DR AlphaFoldDB; A0A0J0YQ91; -.
DR STRING; 1470200.PL75_09080; -.
DR PATRIC; fig|1470200.3.peg.776; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000036027; 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:0000313|EMBL:KLT72300.1};
KW Cell division {ECO:0000313|EMBL:KLT72300.1};
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:UP000036027}.
FT DOMAIN 3..163
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 270 AA; 29520 MW; 3ABCBC7F0F1208D4 CRC64;
MAKIIVVTSG KGGVGKTTTS ASIATGLALR GHKTAVIDFD VGLRNLDLIM GCERRVVYDL
INVIQDEATL NQALIKDKHC DNLFILPASQ TRDKDALTQE GVEKVLKTLT EEMGFDFVIC
DSPAGIEQGA LMALYFADEA IVTTNPEVSS VRDSDRILGI LQSKSRKAEN GETVKEHLLI
TRYSPERVEK GEMLSVQDIC DILRIPLIGV IPESQNVLQA SNAGSPVIHQ NDAVAAEAYK
DVVARLLGEN REMRFLEAEK KSFFKKLFGG
//
