ID A0A1M4ZKT1_9CLOT Unreviewed; 262 AA.
AC A0A1M4ZKT1;
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=SAMN02745158_02817 {ECO:0000313|EMBL:SHF18578.1};
OS Lactonifactor longoviformis DSM 17459.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Lactonifactor.
OX NCBI_TaxID=1122155 {ECO:0000313|EMBL:SHF18578.1, ECO:0000313|Proteomes:UP000184245};
RN [1] {ECO:0000313|EMBL:SHF18578.1, ECO:0000313|Proteomes:UP000184245}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17459 {ECO:0000313|EMBL:SHF18578.1,
RC ECO:0000313|Proteomes:UP000184245};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQVI01000015; SHF18578.1; -; Genomic_DNA.
DR RefSeq; WP_072852824.1; NZ_FQVI01000015.1.
DR AlphaFoldDB; A0A1M4ZKT1; -.
DR STRING; 1122155.SAMN02745158_02817; -.
DR OrthoDB; 9773088at2; -.
DR Proteomes; UP000184245; 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 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:UP000184245}.
FT DOMAIN 3..158
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 262 AA; 28647 MW; C2CB63C0FD61A194 CRC64;
MSEIIVVTSG KGGVGKTTVV ANIGTGLAQL DKKVVVVDTD IGLRNLDVVL GLENRIVYNL
IDVIEGNCRL KQALIKDKQY GSLYLLPSAQ TRDKTAVTPE QMIKLTQELS KEFDYIILDC
PAGIEQGFKN AIAGADRAIV VTTPEVSAIR DADRIIGLLE ANEMEDIQLI INRLRPDMIK
RGEMMSIDDV TDILAVSLLG AVPDDEEVVI ATNQGEPLCG KESLSGQAFS NICRRIQGEE
VPLLDFEVKK GVFRRLGSFF KK
//
